BIO-INORGANIC CHEMISTRY

CLASS NOTES BY KULDEEP GARG FOR CSIR NET/

GATE/ IIT JAM/TIFR/BARC/GSI
(KD SIR)

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KULDEEP GARG CHEMISTRY (KDSIR)

1
 BIO - INORGANIC
(LECTURE-1)
 We will study Bio – inorganic in following steps:
1. Basic introduction
Porphyrin ring, chlorin ring, corrin ring, bacteriochlorin ring ; spectral properties of porphyrin
ring.
Note: Hamari body ke ander jo reactions hoti hain unko chemical reaction ni kehte, metabolism
kehte hain.
Reason why we study bio – inorganic :
 Ham ye dekhte hain ke hamre chemistry ke kon konse metal use ho rahe hain body me aur
kahan kahan use ho rahe hain and kaise kaise work kr rahe hai. Agar ham unki concentration
badhaenge ya ghataenge to hamare body pe kya farak pad raha hai.
 Even hamari body ka blood pressure bhi maintain na rahe to body me problem ho jati hai.
 In general, hamare har body part ki khurak hai Oxygen. Jab oxygen lungs me jati hai to lungs
me pressure high ho jata hai. Jab oxygen lungs me ander jati hai to usse hemoglobin accept
krta hai ar ye Hb tabhi accept krega oxygen ko, jab lungs me pressure high hoga. Higher
pressure me oxygen ki binding sabse achhi hemoglobin ke sath hoti hai.
KULDEEP GARG CHEMISTRY (KDSIR) 2
 Agar oxygen ka pressure lungs me kam hota hai to wo body me ni ja pati. Bas lungs se hi
bahr aa jati hai kyun ke wo hemoglobin se bind ni ho paati low pressure pe.
 Ab puri body me to high pressure reh ni sakta oxygen ka ar hemoglobina kehta hai ke jab
tak sare organs ko oxygen de ni dunga tab tak oxygen ko chhorunga ni, to hemoglobin
jakr oxygen myoglobin ( present in muscles) ko de deta hai.
 hemoglobin and myoglobin hote ek hi cheez hain but difference ye hai ke myoglobin low
pressure pe binding krta hai ar hemoglobin high pressure pe binding krta hai.
This means myoglobin lungs se ni utha sakta oxygen aur hemoglobin destination pe ni de
sakta oxygen.
 Agar blood pressure low ho jaye to myoglobin ki binding aur bhi zyada increase ho jati
hai. Aisa hone ki wajh se myoglobin oxygen ko leke baith jaega ar jis jis ko deke aani thi
oxygen, usko ni deke aaega.
 Agar blood pressure high ho gya to myoglobin bind ni krega oxygen ko ar hemoglobin ko
bolega tu hi aaja. Ab iss case me bhi jahan jahan myoglobin ko oxygen deni thi, whan de
ni paega.
 Blood pressure chahe high ho ya low ho, dono hi case me oxygen puri body ko ni mil pati
ar jiski wajh se chakkar aane lagte hain.
KULDEEP GARG CHEMISTRY (KDSIR) 3
 Myoglobin ki binding capacity ek pressure pe achhi hoti hai. Low pressure hoga to zyada
binding kr lega ar high pressure hoga to bind hi ni krega myoglobin.
 Jab normal blood pressure hota hai to myoglobin hi bind krta hai, hemoglobin bind ni krta.
 Jaise pressure uper neeche hone se dikkat ho jati hai, waise hi agar metal uper neeche ho jaye,
tab bhi dikkat ho jati hai.
 Jaise Fe hai hemoglobin me, kabhi kabhi Fe damage hone lagte hain means met-hemoglobin
banna shuru ho hate hain. Ab naye Fe ki need hoti hain toTransferrin bhagta hai pet me jata
hai ar jo bhi khaya hota hai hamne , usme se Fe nikal ke leke aata hai ar ferretin tak
pahunchata hai.
 Agar salt zyada ho jaye to acid zyada banega . Jab salt zyada ho jata hai to salt se water banne
lagega to wo water blood me chala jata hai. Fir wo water hemoglobin ar myoglobin me chala
jata hai ar unke iron ko bekar kr deta hai. hemoglobin ar myoglobin ke iron water se bind kr
lete hain ar fir oxygen ni utha te .
 Kehte hain hematin banna shuru ho gya, usse met hemoglobin kehte hain. Body me jitna zyada
hematin banna shuru ho ajega , utni hi body bekar hoti chali jaegi.
 hemoglobin sara ka sara globin protein chain se dhaka rehta hai taki water na ghus jaye kyun
ke Hb ko oxygen se bind krna hai na ki water se. Pr fir bhi thoda sa water ghus hi jata hai. Agar
water ghus jaega to Fe ko bekar kr dega.
KULDEEP GARG CHEMISTRY (KDSIR) 4
 hemoglobin rehta to water medium me hi hai but ye jo α and β chain hain amino acids ki ye Fe
ko protect krke rehti hain taki water na kharab kr de Fe ko.
We will study Bio – inorganic in following steps:
1. Basic introduction
• Porphyrin ring, chlorin ring, corrin ring, bacteriochlorin ring ; spectral properties of porphyrin
ring.
2. Oxygen transport and oxygen storage
We will study in both vertebrates and invertebrates.
3. Metal transport and metal storage
Jab oxygen transport padhte hain to kahin na kahin metal kam padte hain. Isliye metal
transport and metal storage padhte hain ham.
4. Electron transfer system
Jab metal transport and metal storage ki baat aati hai to wahan electron tranfer ki baat hoti
hai. Ya to oxidation hota hai ya reduction. To aisi gadiya hongi jo electron ko idher udher le jati
hongi, isliye ham padhenge electron transfer and electron storage. Kyun ke kai baar hota hai ke
O2 kehta hai metal se ke m to ni judunga tere se, apni oxidation badha pehle ya me judunga to
apna ek electron kam kr pehle ya ek electron badha pehle. To Fe ko uske according electron ki
need hogi.
KULDEEP GARG CHEMISTRY (KDSIR) 5
5. Metalloenzyme
 Hamare ander enzymes ki reaction hogi. Jab ham bahot khate hain ar mote ho jate hain mtlb
thk se waste ni nikal rha body se ar metabolism kam ho raha hai. Waste me koi cheez tab hi jati
hai jab wo water soluble ho. Cytochrome P 450 monooxygenase ka kaam krta hai. Ham jo fat
kha rahe hain wo water me soluble ni hota to Cytochrome P 450 uss fat pe oxygen chipkata
rehta hai ( means monooxygenate krta hai ) taki wo fat polar ban sake ar water soluble ho
jaye.
 To hamko aise enzymes padhne hain jo hamare body me trh trh ke kaam krte hain hame zinda
rakhne ke liye, jinko ham kehte hai metalloenzymes.
 Agar koi R—H hai ar uspe Cytochrome P 450 daal den to R—H, R—OH me convert ho jaega.
This explains Cytochrome P 450 ne R—H ko monooxygenate kr diya ar ab polarity badh gyi.
R—OH water soluble hai to waste me bahr nikal jaega.
 Jab ham chicken ya mutton khate hain to uske sath raw onion and gralic khate hain pr fish ke
sath ni khate. Iske peeche scientific reason hai. Chicken ar mutton saturated fat hote hain to
water me easily soluble ni hota. Onion me sulphur ka amount zyada hota hai to wo jake
saturated fat ki polarity ko badhata hai. Ar isliye saturated fat easily digest hota hai.
Fish me unsaturated fat hota hai to uske liye hame onion ki need ni hoti ar itna kaam hamara
Cytochrome P 450 kr deta hai.
KULDEEP GARG CHEMISTRY (KDSIR) 6
6. Nitrogen fixation
7. Photosynthesis
8. Metal used in medicine
For example: Pt is used in cancer drugs.
I is used in thyroid.
9. Na+ / K + pump / Ionophores
 Ca and Mg same group hain but cell ke ander ye different property show krte hain.
Similary, K and Na.
 Cell ke ander K ki concentration zyada hoti hai ar cell ke bahr Na ki. (GATE)
 Jab hame current lgta hai to sabse pehle Na+ / K + pump hi disturb hote hai through
ionophores. Tabi hamara pura shareer kanpne lagta hai ar Na+ / K + ki concentration
kharab hone lagti hai.
10. Toxicity

Note: Hydrolysis metalloenzyme me cover ho jaega.

KULDEEP GARG CHEMISTRY (KDSIR) 7
Basic introduction
Porphyrin Ring
 It is found in human body
 Natural Ligand
 Cyclic Ligand
 Aromatic in nature (follow huckel rule)
 Highly stable (jo aromatic compound hote hain wo highly stable bhi hote hain )

KULDEEP GARG CHEMISTRY (KDSIR) 8

KULDEEP GARG CHEMISTRY (KDSIR) 9
KULDEEP GARG CHEMISTRY (KDSIR) 10
 Ye jo red colour se double bond show kiye hue hain ye conjugation se extra bond lage
hue hain.
 Agar exam me ye puchhe ke how many π –bond or π –electrons are present in porphyrin
ring?
To answer hoga : π –bond = 11
π –electrons = 22
 Since pyrrole is aromatic ar exam me puchh le ke ( 4n + 2) π –electrons me ‘ n ‘ ki value
kya hogi?
Iss case me jo red colour se double bond show kiye hue hain, wo ni include kiye jate.
Number of π –bonds in cyclic conjugation in porphyrin ring = 9
Number of π –electrons in cyclic conjugation in porphyrin ring = 18
( 4n + 2) π –electrons = 18 . Therefore, ‘n’ = 4
 Agar proof mannga jaye ke ye red colour wale double bond conjugation me ni hote to ?
Ans : Agar conjugation me hote ye double bonds to easily reduce ni hote pr ye dono
bonds easily reduce ho jate hain kyun ye dono bonds hamare aromatic system me
participate hi ni kr rahe hain.
KULDEEP GARG CHEMISTRY (KDSIR) 11
 Porphyrin ring me Hydrogen ki 3 position hoti hain.
1. N—H
2. Meso hydrogen
3. β –hydrogen
 Meso hydrogen jo hain porphyrin ring me wo formaldehyde ke H se aate hain. Agar iss position
pe CH3 hota to porphyrin ring me meso position pe H ki jagh CH3 laga hota.

 Number of meso hydrogen = 4

 Number of β –hydrogen = 8
 Number of N—H hydrogen = 2
 Number of signals in 1H—NMR = 3
 Peak of β –hydrogen in 1H—NMR at approx 9 ppm.
Peak of meso hydrogen in 1H—NMR at approx 4 – 5 ppm.
Peak of N—H hydrogen in 1H—NMR at approx -2 ppm. (kyun ke ye hydrogen ring ke ander
hote hain ar shielding effect show krte hain )
KULDEEP GARG CHEMISTRY (KDSIR) 12
KULDEEP GARG CHEMISTRY (KDSIR) 13
UV Spectroscopy
 UV Spectroscopy valence shell ke liye hoti hai. Yahi dfference hai X-ray spectroscopy me
ar UV-spectroscopy me.
 UV spectroscopy me jo electron transition hota hai, wo valence electron ka hota hia.
 X-ray spectroscopy me jo electron trnsition hota hai, wo inner shell ka electron hota hai.
 Jab ham nuclear chemistry padhte hain to wahan ek term aati hai e– capture / K –
capture.

K – capture ka mtlb hota hai jab iss electron ko nucleus capture kr lega to yahan se ek
energy emit hogi, jisse X – ray kehte hain. Agar X – ray yahan se emit hui hai to X – ray
kaam bhi yahi kregi.
KULDEEP GARG CHEMISTRY (KDSIR) 14
 Valence shell me jo electron ka transition padhte hain wo ham padhte hai σ σ*,
π π* , n b σ* , nb π*

σ*

π*

nb

Order of energy for the above transition (TIFR)

σ σ* > n b σ* > π π* > n b π*
KULDEEP GARG CHEMISTRY (KDSIR) 15
 Range of UV = 400 – 700 nm.
 Jo transition UV ki range me aate hai, ham sirf wahi transitions padh sakte hain iss spectrum
me. σ-transition bhi hote honge porphyyrin ring me but wo UV ki range me ni aate to wo ni
dikhte iss spectrum me.
 Isme UV ki range me transitions jo aate hain wo hain: π π* , nb π*
 Porphyrin ring ka UV spectra aisa dikhta hai.

Jo π π* transition hota hai usse bola jata hai Sorat Band.

Jo nb π* transition hota hai usse kehte hain Q – band.
KULDEEP GARG CHEMISTRY (KDSIR) 16
 Porphyrin ring me jitne bhi π –bonds hain, wo sab π π* transition krenage ar nb π*
transition sirf 2 hai because 2 N pe hi lone pair hai. To obviously Sorat band ki intensity
zyada hogi because number of π π* transitions zyada hai.
 Itne sare π π* transition honge to sabki peaks hongi ar itni sari peaks ko ikkatha
band maan lete hain.
 Energy and intensity dono alag alag cheez hain.
IR Band
 IR Band me peaks to bahot sari aaengi pr hame sirf N—H wali peak ka dhyan rakhna hota
hai. Ye peak aati hai approx 3300 cm-1 ke pass.

Note:
 Porphyrin ring se metal judta hai to dianion se judta hai. Jab porphyrin ring me base dalte
hain to wo N se jude dono H ko le leta hai ar ab ye ring dianion ring ban jati hai.
 Agar acid dalenge porphyrin ring me to dication banega ar agar base dalenge to dication
banega.
KULDEEP GARG CHEMISTRY (KDSIR) 17
 Agar porphyrin ring ke NMR me se N—H wali peak gayab ho jati hai to hame pta chalta
hai ke porphyrin ring se metal jud gya.
 UV spectra se Q- band gayab ho jata hai jab metal jud jata hai porphyrin ring se. Jab metal
aake jud to N ke jo lone pair theKULDEEP
wo donate kr diye(KDSIR)
GARG CHEMISTRY gye to Q- band ki peak gayab ho jaegi.
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 IR spectra se N—H wali peak jo 3300 cm-1 ke pass hoti hai, wo gayab ho jati hai jab metal
judta hai prophyrin ring se.
 Jab metal aake judta hai ring se to wo chahta hai ke wo plane m rahe ring ke sath. To
plane me rehne ke liye metal – ligand bond distance ko approx 200 pm hona chahiye.
Agar ye distance 200 pm se zyada hogi to metal plane me ni rahega, wo plane se bahr
nikal jaega. Yahi reason hota hai hemoglobin ka Fe porphyring ring ke ek dam plane me ni
hota.
 Order of best binding of metal with porphyrin ring
Ni+2 > Cu+2 > Co+2 > Fe+2 > Zn+2 (Order of stability on the basis of
(196pm) (210 pm) planarity)

Fe thoda sa tensed hota hai. Pr jab ye O se bind krta

hai to iski oxidation state change hoti hai ar ye plane
me aata hai. Hypothetically oxidation change hoti hai
pr real me change hoti hai ya ni ye aaj tak kisi ko ni
pta.
KULDEEP GARG CHEMISTRY (KDSIR) 19
 BF3.OEt2 me F electronegative atom hai jo electrons ko apni trf kheench ke rakhta hai ar B
ko ek dam electron deficient bna deta hai, jiski wajhse ye H ko accept krne ka kaam krta
hai.
Chlorin Ring (Chlorin A)
 It is found in plants.
 It is found in chlorophyll.

KULDEEP GARG CHEMISTRY (KDSIR) 20

Bacteriochlorin Ring (Chlorin B )

KULDEEP GARG CHEMISTRY (KDSIR) 21

 Porphyrin ring 11 π –bonds
Chlorin ring 10 π –bonds In (4n + 2) π –elctrons : n = 4
Bacterialchlorin ring 9 π –bonds
Iso Bacteriochlorin Ring
 ‘Iso’ mtlb jin N pe H laga hua
tha ab wo wali rings side by
side aaengi.
 Ab bacterio ring hai to 2 extra
π –bonds ni honge.
 Total π –bonds = 9
 Aromatic.

KULDEEP GARG CHEMISTRY (KDSIR) 22

 Porphyrin ring
Chlorin ring Inn sabhi rings se agar metal jud jaye to inn rings me
Bacterialchlorin ring 4 rings 5-memebered hain ar 4 rings 6-membered
Iso Bacteriochlorin Ring hain.
Ye sari 16 membered macrocyclic ring hain. Jinn jinn
pr mark kr rakha hai wo sabi atom macrocyclic ring
me include honge. In other words, β-hydrogen wale
carbon ko chhor ke sabhi macrocyclic ring me include
honge.
Macrocyclic ring puchhe ya in general kitne
membered ring hai, ye puchhe to answer hoga 16.

KULDEEP GARG CHEMISTRY (KDSIR) 23

 BIO - INORGANIC
(LECTURE-2)
Corrin Ring
 Ar rings ke comparison me corrin
ring me ek jagh 2 pyrrole rings ke
beech me direct connection hoga.
Ar jahan pr ye direct connection hoga,
bas wahan pr ek N—H wala hydrogen
hoga. Baki teeno N pe lone pair honge.
 Jahan ye direct connection hua hai 2
pyrrole rings ke beech , uss side ( jo
alag se red se highlighted hai) dono
N me se kisi pe bhi C—N double bond
ni aaega.
 Jiss ring me N—H hai uss ring me koi
conjugation ni hai. Hence. Corrin ring
is non-aromatic.
KULDEEP GARG CHEMISTRY (KDSIR) 24
 Number of π –bonds in corrin ring = 6 π –bonds .
 Corrin ring vitamin B12 co-enzyme me paayi jati hai.
 If metal gets attached to corrin ring :
Number of 5- membered rings = 5
Number of 6-membered rings = 3

KULDEEP GARG CHEMISTRY (KDSIR) 25

Question 1:
How many 5-membered and 6-membered rings are present in Tetra benzo porphyrin ring?
Ans: Number of 5- membered rings = 8
Number of 6-membered rings = 4

KULDEEP GARG CHEMISTRY (KDSIR) 26

Question 2:
What is porphyrazine ring? (BARC)
Ans:
Number of π –bonds = 11
Number of π –electrons = 22

KULDEEP GARG CHEMISTRY (KDSIR) 27

Corphin Ring
 Isme N—H ke dono trf double bond hota hai ar teeno N pe ek ek double bond hota hai.
 Corphin ring is found in co-enzyme F 430.
 YE jo enzyme F 430 me 430 hai, ye represent krta hai ke iska absorption 430 pe hota hai
ar ye range UV me aati hai. This means ye number spectra ko darshata hai.

KULDEEP GARG CHEMISTRY (KDSIR) 28

Oxygen Transport and Storage
 If we talk about oxygen transport and storage , there are 4 protein chains namely hemoglobin,
myoglobin, hemerythrin, hemocyanin which work for oxygen transport and storage.
 hemoglobin(Hb), myoglobin(Mb) to human body me paayi jati hain.
Hemerythrin is found in marine invertebrates.
Hemocyanin is found in some invertebrate animals.
 Tissues ki khurak O2 hoti hai, hemoglobin lungs se O2 ko high pressure and high pH pe uthata
hai (means bind krta hai O2 ke sath).
 Fe + porphyrin ring ke 4 units (ye 4 units apas me jude hote hain) ko ek sath hemoglobin kehte
hain ar inme se ek unit ko myoglobin kehte hain.
 hemoglobin oxygen leke jata hai tissues ke pass wahan jake Hb ki O2 ki binding tutne lgti hai
due to low pressure and low pH. Pr tissues me Mb hota hai jo uss oxygen se bind kr leta hai.
 High pressure and high pH me O2 ki binding Hb ke sath achhi hoti hai. Ar low pressure and low
pH me O2 ki binding Mb ke sath achhi hoti hai.
Hence, Hb works as oxygen tranport (lungs se tissue tak) and Mb works as oxygen storage. Mb
tissue me oxygen ko rakh ke baith jaega. Fir ab sab Mb se oxygen maangte hain to Mb sabko
oxygen banta hai.
KULDEEP GARG CHEMISTRY (KDSIR) 29
 Fe= O2
Mb
hemoglobin O2

Pressure Tissue Pressure

pH pH
 Ab myoglobin ne O2 se binding kr li to ab wo CO2 ko chhor dega.
 Ab iss CO2 ke bahr nikalne ke 3 tareeke hai.
1. Dissolve hoke nikal jaye. (Isse 7% CO2 bahr nikal ke jati hai)
2. Ion ki form me nikal jaye. (bahot sari CO2 ion (HCO3–) ki form me bahr nikalti
hain, about 70%).
3. hemoglobin ke sath nikal jaye. (23% CO2 ko Hb leke jata hai)
CO2 ka ion ki form me bahr nikalna
Carboxy anhydrase Ye process cell
 H2O + CO2 H2CO3 ke ander ho raha
 Water ki presence me H2CO3 convert ho jata hai H+ and HCO3– me. hai.
KULDEEP GARG CHEMISTRY (KDSIR) 30
 Cell ke bahr Cl – wait kr raha hai. To Cl – cell ke ander jata hai ar HCO3– ion form me cell se
bahr aa jata hai ar dissolve hoke lungs tak jata hai, pr H+ to abhi bhi cell ke ander hi hai.
 Cell ke ander itna carboxy anhydrase ni hota ke sare CO2 ko H+ and HCO3– ki form me bahr
kr de. Cell ke ander carboxy anhydrase ki matra kam hoti hai.
 Ab HCO3– to chala gya cell se bahr ar ar ander H+ as it is bach gya. Ab yahi bacha hua H+
RBC ke ander H+ ki concentraion badha deta hai ar medium ki pH low ho jati hai. Jo
hemoglobin aaya hota hai oxygen leke, uske sath jo protein lagi hui hai, uspe NH2 laga
hota hai , jo H+ ko dikh jata hai ar wo NH2 se jud ke NH2+ bna leta hai ar Hb ko O2 chhorne
pe majboor kr deta hai. Jaise hi NH2+ banta hai to kuchh CO2 uspe judne lagti hai.
 Ye jo H+ ki concentraion increase hone se pH low hoti hai , issi ki wajh se Hb O2 ko
chhorne pe majboor ho jata hai. Kyun low pH pe Hb ki O2 se binding achhi ni hai. Ar iss O2
ko myoglobin le leta hai. Jo cell me CO2 hoti hai jisse carboxy anhydrase convert ni kr pata
H+ and HCO3– me, wo CO2 Hb ke sath bind hoke bahr nikal jati hai. To aise CO2 Hb ke sath
bahr nikalti hai (approx 23%).
 Kuchh CO2 water ke sath dissolve hoke nikalti hai, jo 7% hoti hai.

KULDEEP GARG CHEMISTRY (KDSIR) 31

 CO2 ke bahr nikalne ke 3 tareeke hai

Disslove hokr Ion form me (HCO3–) hemoglobin se chipak kr

(7%) (70%) (23%)

Isse Chlorine shift bhi kehte hai

Question 3:
Oxymyoglobin ar deoxymyoglobin me Fe ki oxidation state kya hoti hai ?
Ans: Deoxymyoglobin = Fe+2
Oxymyoglobin = Fe+2 (ye Atkins me diya hua hai).
But ham ye ni padhenge we will consider oxydation state to be +3. Hamare pass +3 ka
reference hai. See the paper of GATE-2012 and NET DEC 2019.
Jahan Atkins me Oxymyoglobin Fe ki +2 oxidation state ki baat likhi hain wahin neeche
likha hai ke oxygen O2– (superoxo form) ki form me judta hai to oxidation state +3 hoti
hai. Oxygen Mb se superoxo form me judta hai, iss baat ka pramar (evidence) hame
Raman spectroscopy se milta hai (Ye baat bhi likhi hui hai).
KULDEEP GARG CHEMISTRY (KDSIR) 32
Question 4:
hemoglobin is an oxygen carrier protien. The correct statement about oxyhemoglobin is that:
(GATE 2012)
(a) The metal is low-spin in +3 oxidation state while dioxygen is in O2– form.
(b) The metal is high-spin in +3 oxidation state while dioxygen is in O2 form.
(c) The metal is low-spin in +3 oxidation state while dioxygen is in neutral form.
(d) The metal is low-spin in +3 oxidation state while dioxygen is in neutral form.
Ans: Ab iss question me +2 oxidation to kahin bhi ni likhi.
Correct option : (a)
 NET DEC 2019 me ek question puchha hai ke kiske unpaired electrons ki sankhya
deoxymyoglobin ke sath match krti hai ar exam me unn options ko correct kiya hai jinme
ek unpaired electron hai. Agar ye d2 system hota to t2g system hota ar unpaired electrons
0 hote.
Disclaimer: Ab agar in future question me aajaye +2 and +3 oxidation state to wo ab student
ka risk hai because samne wale ka koi pata ni ke konsi line ko wo consider krega ar konsi
line ko consider ni krega.
KULDEEP GARG CHEMISTRY (KDSIR) 33
hemoglobin
 Ab tak hamne padha tha ke hemoglobin me Fe ar N (of porphyrin ring) ke beech ki
distance 200 pm honi chahiye taki Fe plane me reh sake. But Fe+2 ar N (of porphyrin ring)
ke beech ki distance 210 pm hoti hai. To iss case me Fe porphyrin ring ke chaaron N ke
sath planarity loss kr deta hai ar bahr nikal jata hai.

 Ab ye bahr nikla hua Fe hai , isko sabse bacha ke rakhna hota hai. Jaise H2O se bachana
hota hai. Agar H2O jud gya to methemoglobin bna lega ar wo kisi kaam ka ni hota.
Issiliye Fe ko lapet k rakhte hain jo kawach ki trh kaam krta hai. Ye hota hai protein +
amino acid, isse kehte hain globin chain.
KULDEEP GARG CHEMISTRY (KDSIR) 34
 Ek hemoglobin me 4 porphyrin ring hoti hain mtlb 4 jagh Fe hota hai. Ab inn 4 me se koi
bhi do α ho skti hain ar koi bhi 2 β ho sakti hain.
 Ek α –chain 141 amino acids se bani hoti hai. Ek β –chain 146 amino acids se bni hoti hai.
 Ye chaaron chain apas me salt bridge se judi hoti hain.
 Ye globin chain me histidine (amino acid) ke imidazole group ka N, Fe se 5th site pe judta
hai.

KULDEEP GARG CHEMISTRY (KDSIR) 35

 Bahot sare amino acids hote hain globin chain me. Jo histidine aake judta hai Fe se, usse
kehte hain “proximal histidine”.
 Abi jab 6th site vacant hai to iss state ko kahenge “tensed state” kyun ki Fe plane me ni hai
because bond distance 210 pm hai.
 Jab O2 aake judta hai to Fe +3 O.S. meGARG
KULDEEP chala jata hai
CHEMISTRY ar plane me aa jata hai.
(KDSIR) 36
 Jab Fe convert ho jaega Fe+3 me to uska size chhota ho jaega to jo bond distance pehle
210 pm ki thi, ab usse kam ho jaegi. Ar ab ye “relaxed state” me aajaega. Ab koi relaxed
state me aa jaega to uska koi cheez chhorne ka mn ni krega.

KULDEEP GARG CHEMISTRY (KDSIR) 37

 Ab jo ar amino acids, unka jo NH2 group hai, uska O=O pe dil aa jata hai (H- bonding). Ar
issi wajh se Fe—O—O ka angle linear na hoke 130° ho jata hai.

 Jab ek O2 aake jud jaega 4 me se 1 unit me to hemoglobin me structural change hote

hain. Jiski wajh se salt bridge tut jata hai. Jaise hi salt bridge tutna start hota hai, dusre
unit pe O2 ar bhi tezi se judne lagta hai. Fir ar salt bridge tut ta hai to teesri unit pe ar bhi
tezi se O2 judne lagta hai. Ar fir 4th unit pe pehle se ar tezi se O2 judne lagta hai. Issi cheez
ko co-operative effect bola gya.
KULDEEP GARG CHEMISTRY (KDSIR) 38
 Structure change hone ki wajhse binding affinity ka badhna, co-operative effect kehlata
hai.

 K1 = First binding constant ; K2 = Second binding constant and so on.

 Rate of binding
K4 > K3 > K2 > K1 (This is co-operative effect )
KULDEEP GARG CHEMISTRY (KDSIR) 39
 Ab ye hemoglobin O2 leke bhaga tissue ki trf. Ab hemoglobin O2 ko chhorna to chahta ni
hai but wahan (tissues) ka jo environment tha, uski wajh se Fe relaxed state se tensed
state me aa jata hai ( means O2 chhor deta hai)
Environment = conc. of H+ , pH or acidic environment.
 This suggests that low pH prefers tensed state. Issi cheez ko Bohr’s effect (tissue ke ander
hota hai) kaha gya.
Oxidation state
Deoxymyoglobin
 Fe+2 Configuration = t2g4 eg2
 Agar iski CFSE nikalne ke liye aa jaye to high spin ke ander pairing energy(P.E.) ko ham
neglect krte hain.
CFSE = 0.4 Δo
Oxymyoglobin
 Ham Fe+3 padhenge oxymyglobin me oxidation state.
 Log Fe+2 bhi padhate jata hain kahin kahin. Uska reason hai ke compound diamagnetic
hota hai ar wo diamagnetic tabhi ho sakta hai jab Fe+2 me ho ar configuration t2g6 eg0 ho
and low spin complex banaye. KULDEEP GARG CHEMISTRY (KDSIR) 40
 Pr hamari nazar jab Raman spectrum pe jati hai to wahan dekha gya ki free O2 molecule
ki stretching frequency 1560-1570 cm-1 pe milti hai. Ar jab Fe se binded O—O bond ki
stretching frequency dekhi to wo milti hai 1150 cm-1 ke aas pass. Aisa tabi hua hoga jab
free O2 molecule ke comparison me bond order kam hoga. 1150 cm-1 pe jo hame B.O.
milta hai wo 1.5 B.O. milta hai ar 1.5 B.O. paya jata hai O2– ke beech me. This means O2 ,
free O2 molecule ke form me judi hi ni, ye judi hai superoxo form (O2– ) me. Isse ye pta
chalta hai ke Fe se O2 superoxo form (O2– ) me judi hai isliye Fe is in Fe+3 state.
 Hamne Raman spectra hi dekha IR ni dekha kyun ke O2 molecule is inactive in IR because
there is no change in dipole moment in O2 molecule. Ar jo IR me inactive hote hain , wo
Raman me active hote hain.
 Ab ye sochne wali baat hai ke Fe+3 diamagnetic kaise hua?
Agar isne low spin bhi bna liya to t2g5 eg0 hoga. Ab ek unpaired electron hai fir bhi
diamagnetic kaise?
Oxymyglobin is diamagnetic due to anti-ferromagnatic coupling. Ab ye sochne wali hai ke
myoglobin me to 1 hi Fe to anti-ferromagnatic coupling kaise krega?

KULDEEP GARG CHEMISTRY (KDSIR) 41

 Jab oxygen judta hai to O2– ki form me judta hai ar iska MOT dekhen to hame kuchh aisa milta
hai:
π* π*

O2 O2 –

 Fe+3 (T2g5 eg0 ) me jo 1 electron unpaired hai uske sath O2– ka 1 unpaired electron couple
(anti-ferromagnatic coupling ) kr leta hai. This is the reason for oxymyoglobin to be
diamagnetic. Hence, ESR inactive.
 Agar O2– Fe+3 ke sath couple ni krta to Fe+3 ke unpaired electron ka dil kisi ar me aa jata hai ar
methemoglobin bna leta hai.
 CFSE of oxymyoglobin = - 0.2 Δo + 2P
Note:
 hemoglobin ka weight approx. 15000 dalton hota hai ar myoglobin ka weight approx. 4000
dalton hota hai.
 hemoglobin 4 porphyrin ring units se milkr bna hai ar myoglobin 1 porphyrin ring unit se milkr
bna hai. hemoglobin ar myoglobin ko almost ek hi baat samjho, alag alag ni.
 Jaise tissues me Bohr’s effect hota hai, waise hi lungs me Haldane effect hota hai. Lungs me
CO2 aa gyi to ab CO2 ko chhorna hai.
KULDEEP GARG CHEMISTRY (KDSIR) 42
 Yahan ek myoglobin ka curve hai
ar hemoglobin ka curve hai.
 Myoglobin pehle hi low pressure
pe saturate ho jata hai.
 Hemoglobin ka curve sigmoida.l curve hai

KULDEEP GARG CHEMISTRY (KDSIR) 43

Question 5:
The metal ion and macro cyclic skeleton present in the green pigment of plants, respectively,
are: (GATE 2017)
(a) Mg(II) and chlorin (b) Mg(II) and corrin
(c) Mn(II) and chlorin (d) Mg(II) and porphine
Ans: Correct option : (a)

Question 6:
The O2 co-ordinated to metal ion in centres in oxy –myoglobin and oxy –hemocyanin exists ,
respectively as: (GATE 2018)
(a) Superoxide and peroxide (b) Superoxide and superoxide
(c) Peroxide and peroxide (d) Superoxide and oxygen
Ans: Correct option to baad me dekhenge pr hamko ye pta hai ke option (c) correct ni hoga.

KULDEEP GARG CHEMISTRY (KDSIR) 44

Question 7:
The νO—O resonance Raman stretching frequency ( in cm-1 ) of the O2 co-ordinated to iron centre in
oxyhemoglobin is nearly:
(a) 1100 (b) 850 (c) 1550 (d) 1950
Ans: Correct option : (a)

Question 8:
Among the given pH values, O2 binding efficiency of hemoglobin is maximun at
(a) 6.8 (b) 7.0 (c) 7.2 (d) 7.4
Ans: Higher pH pe achhi binding efficiency hoti hai hemoglobin ki O2 ke sath.
Correct option : (d)

Question 9: (GATE 2013)

Oxymyoglobin and oxyhemoglobin, respectively are:
(a) Paramagnetic and paramagnetic (b) Diamagnetic and diamagnetic
(c) Paramagnetic and diamagnetic (d) Diamagnetic andparamagnetic
Ans: Correct option : (a) KULDEEP GARG CHEMISTRY (KDSIR) 45
Question 10: (GATE 2009)
In transformation from oxyhemoglobin to deoxyhemoglobin :
(a) Fe3+ in the low spin state changes to Fe2+ in the high spin state.
(b) Fe2+ in the low spin state changes to Fe3+ in the low spin state.
(c) Fe2+ in the high spin state changes to Fe2+ in the low spin state.
(d) Fe2+ in the high spin state changes to Fe3+ in the high spin state.
Ans: Correct option : (a)

KULDEEP GARG CHEMISTRY (KDSIR) 46

 BIO - INORGANIC
(LECTURE-3)
Hamne hemoglobin / myoglobin ko protein chain (globin chain) se kyun lapet diya?
 Globin chain ke 2 part hote hain. Ek part hota hai hydrophilic(water loving) ar dusra part
hota hai hydrophobic.
 Agar globin chain ni lagai hamemoglobin ke uper to to hemoglobin ke uper water chipak
jaega ar hemoglobin O2 ni carry kr paaega. Water chipak gya hemoglobin pe to cells me
water deCO2ficiency ho jaegi ar isski wajh se cell me jo hai wo water ke sath bind ni ho
paegi ar na hi HCO3– ban kr cell se bahr nikal paegi. To CO2 accumulate hoti rahegi cells
me. Aisa na ho issi liye hemoglobin civered rehta hai globin chain se.
 Globin chain ka hydrophilic part bahr ki trh hota hai (body me water content sabse zyada
hai to ek jagh se dusri jagh jane ke liye hemoglobin ko water me hoke hi jata hoga to
water ke sath bonding honi zaruri hai globin protein ki) ar hydrophobic part ander ki trf
rehta hai.

KULDEEP GARG CHEMISTRY (KDSIR) 47

 Maan lo agar water na jude hameoglobin ke Fe se, tab bhi importance hai globin protein
ki. Hamko pta hai jab O2 judti hai hemoglobin se to superoxo form me judti hai (O2–).
Isliye attached oxygen pe -1 charge hota hai.
Fe—O—O–
Hme pta hai ke pehle reaction charged species me hoti hai. To dusra hemoglobin dusri
oxygen me lane ki jagh already attached O2 se jud jaega. Ab dono me se koi bhi
hemoglobin O2 ko chhorne ke liye taiyar na ho. To isse ek cheez ready ho gyi ar wo hai
met hemoglobin.
Fe—O—O—Fe

Isse Met hemoglobin banega.

 Globin chain hemoglobin ko 2 cheezon se bachati hai.
1. Hydrate hone se bachata hai hemoglobin ko.
2. Met hemoglobin banne se bachata hai.

KULDEEP GARG CHEMISTRY (KDSIR) 48

Met hemoglobin
 Jahan Fe likh rahe hain wahan porphyring present hai usko sang leke chalna hai. Yahan
complexity ki wajh se show ni ki hai.
Fe + O2 Fe (III)—O
O
Fe (II)

Fe (III)—O—O—Fe (III) 2 Fe (IV) O

Fe (IV) O + Fe (II) Fe (III)—O—Fe (III)

Met hemoglobin
 Agar met hemoglobin ban rahi hai body me to iska mtlb ham jaldi beemar pdenge. Ham
kehte hain ke haemglobin khatam ho raha hai, it means wahn met hemoglobin ban raha
hai.
KULDEEP GARG CHEMISTRY (KDSIR) 49
 Met hemoglobin bna to Fe ki deficiency ho jati hai. ‘Fe’ body me present hai but kisi
kaam ka ni hai.
 Jitne zyada superoxo form(O2–) ban rahe hain , utne met hemoglobin banne ke chance
zyada hai. Isliye ham ek enzyme use krte hain, ‘superoxo dimutase’ (SOD). Iss enzyme ka
kaam superoxo form (O2–) ko khatam krna hai.
 Ye superoxo dimutase (SOD), do baar O2– ko leta hai. Ek baar O2– leta hai to O2 nikalta hai
ar dusri baar O2– leta hai to H2O2 nikalta hai. Isliye iss enzyme ko dimutase kehte hain.
 Superoxo dimutase (SOD), O2– ko O2 and H2O2 me convert kr deta hai. Ab ye jo hydrogen
peroxide bna hai, iske liye body ek enzyme produce krti hai, jiska naam hai ‘peroxidase’ or
‘catalase’ .
 Hamne shuru me padha tha ke H2O ko rokne ke liye globin chain se water protection kr
rakhi hai but ab water ko kitna hi koi rok lega, thoda water to riss kr ke ander aa hi jaenga
Fe se judne . Issi ko ‘peroxidase’ kehte hai. Mtlb hemoglobin me Fe ki 6th position se jab
water jud jayee, uss ko peroxidase bolenge.Ar Fe ki O.S. ho jaegi +3. Isliye kehte hain kisi
bhi cheez ki excess bhi bekar hai ar bilkul na hona bhi bekar hai. Koi bhi cheez ek
balanced amount me honi chahiye.
 Peroxidase, H2O2 ko O2 me convert kr deta hai.
KULDEEP GARG CHEMISTRY (KDSIR) 50
 Hamne padha tha ke CO2 three forms me bahr nikalta hai.
1. Dissolve hoke (7%)
2. Hb ke sath jud kr (23%)
3. Ion (HCO3–) form me (70%)
 Iss ion (HCO3–) form ko banane ka kaam ‘carbonic anhydrase’ krta hai.
 Jo CO2 dissolve hoke ja raha tha, wo water ke sath dissolve hoke ja raha tha. Ab jate jate
raste me CO2 ko NH3 (ammonia) se pyar ho gya ar isnhone bna liya urea(NH2—CO—NH2).
 Iss urea ki wajh se haddiyon me drd hota hai jab khade hote hain to ar per neeche
zameen pe ni rakha jaega. Ab agar ye ure dissolve ho jaye to urine ke through nikal jaye.
To ab enzyme aata hai ‘urease’.
 Urease kehta hai, CO2 and NH3 , tum dono pyar ni kr skte ar urinase convert kr deta hai
urea ko wapis CO2 and NH3 me.
Urease
NH2—CO—NH2 CO2 + NH3

KULDEEP GARG CHEMISTRY (KDSIR) 51

 Ab ye peroxidase itne acche se H2O2 ko convert ni kr paata O2 me. Kafi logon ki body me
H2O2 zyada banta hai. To ham ye krte hain ke Fe ke sath jo 5th position pe Histidine amino
acid juda hua hai, uski jagh Tyrosine laga dete hain ar ab ye enzyme ban jata hai ‘Tyrosine
catalase’.
Tyrosine catalase
H2O2 O2
 Ab tak hamne following enzymes padh liye.
1. Superoxo dimutase
2. Peroxidase
3. Tyrosine catalase
4. Carbonic anhydrase
5. Urease

KULDEEP GARG CHEMISTRY (KDSIR) 52

 R—OH Aldehyde
(1 °Alcohol) Liver alcohol dehydrogenase (LADH)

 2 °Alcohol Ketone
Liver alcohol dehydrogenase (LADH)
 Jiski body me ‘Liver alcohol dehydrogenase (LADH) ’ achhe se banta hai usko kam chadhti
hai.
 Alcohol pe LADH kaam krta hai to aldehyde banta hai ar ye aldehyde mitochondira ke
ander chala jata hai fir wahan aldehyde ko acid me convert krne ka kaam ‘aldehyde
dehyrogenase(ALDH) ’ krta hai.
 Jab koi bahot hi drunk hota hai to doctor antacid lagate hain.

KULDEEP GARG CHEMISTRY (KDSIR) 53

Carboxy peptidase
 Koi bhi peptide chain hoti hai to uske terminal pe jahan NH—CO bond hota hai, usko
beech me se tod deta hai.
O
—NH—C—
Xanthine Oxidase
 Ye pathri ko dissolve krke bahr nikalta hai. Xanthine ko dissolve krke bahr nikalta hai.
Xanthine Oxidase, xanthine ko polar banata hai ar aise ye xanthine ko water soluble
banata hai. Xanthine ko uric acid me convert kr deta hai. Tabhi kehte hain pathri urine ke
through bahr nikalti hai.
 CP CA LADH
(Carboxy peptidase) (Carboxy anhydrase) (Liver alcohol dehydrogenase )
Inn teeno me Zn use hota hai.
Trick:
 CA sabko saanp (snake) ki trh das lete hain (Disclaimer: Just to remember chemistry). Ar
saanp ki awaz hoti hai Hissss Hissss. Isss ham yaad rakhenge ke carboxy anhydrase me Zn
se 3 Histidine group jude hue hain.
KULDEEP GARG CHEMISTRY (KDSIR) 54
 CP (carboxy peptidase) ko ham yaad rakhenge CP (Cannaught Place ) se. CP me CA ke
comparison me 3 me se 2 His (Histidine) to bachenge ar 1 Glu (Glutamic acid).
Isko yaad krne ki trick : 2 Histidine, Glu se chikap (CP) gye.
 LADH me His , Cis, Cis. This means Zn+2 se 1 Histidine juda hai ar 2 Cistine.
 CP CA LADH
Inn teeno me Zn+2 present hota hai; teeno enzyme tetrahedral ; sabki hybridization
sp3.
Summary
CP His, His, Glu
CA His, His, His Zn+2 , Td , sp3
LADH His, Cis, Cis

KULDEEP GARG CHEMISTRY (KDSIR) 55

Xanthine oxidase (XO)
Xanthine oxidase me metal use hoti hai: Mo, wo bhi (VI) or +6 oxidation state me.
 Xanthine oxidase me Mo se 2 unit Fe2S2 ki judi hoti hai. Ye Fe2S2 (ferredoxin) electron
transfer me aata hai.
 Xanthine oxidase, Xanthine ko uric acid ( water soluble) me covert krta hai.
Xanthine oxidase
 Xanthine Uric Acid
Aldehyde oxidase (AO)
Aldehyde oxidase
R—OH R—CHO R—COOH
 Aldehyde oxidase me Mo use hoga ar +6 (VI) oxidation state me.
 Aldehyde oxidase ander Fe2S2 (ferredoxin) ki 2 units hoti hain.
Summary
XO and AO Mo+6
XO and AO Electron transport system = Fe2S2 (ferredoxin)
KULDEEP GARG CHEMISTRY (KDSIR) 56
 Xanthine oxidase ne uric acid bna diya xanthine se. Ar fir issi uric acide se urea ban jaega, fir iss
urea ke liye urease enzyme use hoga.
Urease
 Ek urease me Ni ke 2 atom hote hain, +2 oxidation state me.
 Kabhi kabhi side group kya lage hain wo pucch lete hain. To side me , ek trf 2 histidine lage
hote hain ar dusre trf 2 histidine and 1 aspartic acid lage hote hain.
 Urease ka kaam hai urea ko ammonia and carbon dioxide me convert krna.

Peroxidase
 Issme Fe, +3 oxidation state me paya jata hai.
 Iss enzyme me haeme group( Porphyrin ring ke beech me Fe ar fe ki 5th position pe Histidine)
present hota hai.
 Issme Fe ki 6th position pe H2O present hota hai.
Catalase
 Peroxidase enzyme me Histidine ki jagh tyrosine laga den to catalase enzyme ban jata hai, ar
ussi ko ham kehte hain tyrosine catalase.
 Kuchh bhi naam likha ho sakta hai: tyrosine catalase ya sirf catalase enzyme bhi likha hota hai.
KULDEEP GARG CHEMISTRY (KDSIR) 57
 Tyrosine lag jane ki wajh se rate of reaction increase ho jata hai ar catalase bahot tezi se
H2O2 ko convert krta hai O2 me.
Summary
CP (Carboxy peptidase)
Zn+2 CA (Carboxy anhydrase)
LADH

Mo+6 XO (Xanthine oxidase) Electron transport system = Fe2S2

AO (Aldehyde oxidase) (ferredoxin)

Ni+2 Urease
Fe+3 Peroxidase
Tyrosine Catalase

KULDEEP GARG CHEMISTRY (KDSIR) 58

Summary of work of above mentioned enzymes
 Carboxy anhydrase (CA)
CO2 HCO3–
 Carboxy peptidase (CP)
Peptide bond ko terminal se break krta hai.
O
—NH—C—
 Liver alcohol dehydrogenase (LADH)
R—OH R—CHO
 Xanthine oxidase (XO)
Xanthine Uric acid
 Aldehyde oxidase (AO)
R—CHO R—COOH
(Acetic acid)
KULDEEP GARG CHEMISTRY (KDSIR) 59
 Urease
Urease
Uric acid Urea CO2 + NH3
 Peroxidase and Tyrosine Catalase
H2O2 O2
 Superoxo dimutase (SOD)
Isme Cu+2 ar Zn+2 hota hai.
SOD are of 3 types:
1. The Cu/Zn types
2. Fe and Mn types
3. The Ni type
Human body me sabse zyada Cu/Zn types SOD paya jata hai. Ar iska kaam hota hai ke wo
O2– ko leke O2 banata hai fir dusre O2– ko dobara leta hai ar H + ki presence me usse H2O2
me convert krta hai.
KULDEEP GARG CHEMISTRY (KDSIR) 60
Note:
SOD Peroxidase/ Catalase
 O2– H2O2 O2

Carboxy anhydrase
 CO2 Bicarbonate

Urease
Urea CO2 + NH3

LADH AO
 R—OH R—CHO R—COOH
XO Urease
 Xanthine Uric acid Urea CO2 + NH3
 Terminal peptide bond break krna ho to Carboxy peptidase ka use krte hain.
KULDEEP GARG CHEMISTRY (KDSIR) 61
Dissociation curve of Myoglobin and hemoglobin
 hemoglobin ka sigmoidal curve aata hai.
 Jab lungs me pressure 100 torr ke aas paas hota hai tabi hemoglobin pura saturate hota
hai.
 Jabki myoglobin 40 torr ke approx pressure hone pe hi saturation aa jata hai. Same
pressure (approx 40 torr) pr hemoglobin me 50% hi saturation aata hai.
 Isliye ham kehte hain ke lungs me pressure high hota hai ar tissues me pressure low hota
hai.

KULDEEP GARG CHEMISTRY (KDSIR) 62

Diagram of dissociation curve of myglobin

KULDEEP GARG CHEMISTRY (KDSIR) 63

 BIO - INORGANIC
(LECTURE-4)
Question 11:
Complex which has/have unpaired electron i.e. equal to Fe centre in oxymyoglobin is/are:
(A) [Fe (ox)3 ]3– (B) [ Fe (CN)6 ]3– (C) [ NiCl4 ]2– (D) [Cu(NH3)4 ]2+
(NET DEC 2019) 4marks
(a) A and B (b) B and D (c) C only (d) C and D only
Ans: Correct option : (b)
ox = oxalate weak ligand Ar weak ligand tab tak pairing ni krta, jab tak +4
oxidation state na ho.
 Koi bhi oxide hoga to wo Co+3 ke sath low spin dega na ki Fe+3 ke sath.
 Iss question wo sab log bhar ho jaenge jo oxymyglobin me Fe ko +2 O.S. me mante hain
because +2 O.S. ka mtlb hai d6 ar zero unpaired electron. Ar yahan zero unpaired electron
ka to koi option hi ni hai.
KULDEEP GARG CHEMISTRY (KDSIR) 64
 Oxymyglobin +3 me paya jata hai to wo low spin hota hai, octahedral species ke sath me.
Ar octahedral me low spin ke sath configuration hota hai : T2g5 eg0 (1 unpaired
electron).
 Ab [Fe (ox)3 ]3– me T2g3 eg2 hoga configuration because yahan weak ligand hai. To yahan
5 unpaired electrons hue, isliye ye option galat.
 [ Fe (CN)6 ]3– me CN– strong ligand hai to configuration hoga T2g5 eg0 and 1 unpaired
electron, to ye correct option hua.
 [ NiCl4 ]2– to pta hi hai Ni+2 d8 hoga ar ye tetrahedral hota hai. Isme 2 unpaired electrons
hote hain. To ye option galat hua.
 [Cu(NH3)4 ]2+ to d9 case hai ar 1 unpaired electron hoga (Huggins concept lagta hai isme).
To ye correct option hai. [Cu(NH3)4 ]2+ square planer complex hai ar isme Huggins concept
lagta hai.)
 Hence, (b) B and D , is the correct option.

KULDEEP GARG CHEMISTRY (KDSIR) 65

Hill constant
 Ham hill constant ko ek example se samjhenge.
 Suppose 3 dost hain, teeno shadi me jate hain ar apni apni speed se 1 plate khana khate
hain. Sabse pehle ek dost jata hai, wo apni speed se 1 plate khana khata hai fir dusra dost
aata hai, ar wo apni speed se 1 plate khana khata hai. Fir teesra dost aata hai ar wo apni
speed se 1 plate khana khata hai. To yahan aisa ni hai ke dusre dost ke aane ki wajh se
pehla dost ar tez tez se khana khane lagta hai. Ar na hi aisa hai ke teesre dost ke aane se
pehle do dost tez tez khana khane lagte hain. Koi bhi aaye sab apni apni speed se hi
khana khate hain.
 Ab ek ar case, yahan bhi 3 dost hain. D1, D2, D3, 3 dost hain.
D1 dost chor ko maar raha hota hai, fir D2 dost aata hai ar wo dekhta hai ke D1 dost chor
ko maar raha hai to D2 bhi chor ko maarne lagta hai. D1 ne D2 ko dekha ke ye chor ko
maar raha hai to D1 ar tez tez chor ko marne lagta hai. D3 aata hai ar dekhta hai D1 and
D2 chor ko maar rahe hain to wo bhi chor ko maarna shuru kr deta hai. Ab teno dost D1,
D2, D3 milke zor zor se chor ki pitai krte hain . To yahan dusre dost ke aane se pehle dost
ki maarne ki speed badh jati hai.
KULDEEP GARG CHEMISTRY (KDSIR) 66
 Hill constant = 1 ka mtlb hai independent to others. Jaisa shadi wala case tha, agar dusra
dost ni aata tab bhi pehla dost 1 plate hi khana khata ar jab wo aaya tab bhi 1 plate hi
khana khaya. To shadi wale case me sare dost ka hill constant = 1 hai.
 Jaise jaise hill constant increase hota hai, waise waise binding affinity badhti hai.
 Jab hill constant =1 hota hai to wo dusron se independent hota hai. Ar jab hill constant 1
se zyada hota hai ya 1 se kam hota hai, to ye dusron pe dependent hota hai.
 Hill constant ‘+’ bhi ho sakta hai ar ‘-’ bhi ho sakta hai.
 Hill constant =1 to equilibrium me ho gya na. Hill constant experimental hai isliye yahan
directly value bta rahe hain. Binding constant ke formula se exxperimental value nikali jati
hai ke iska hill constant kya hai. Hill constant ka concept samjhaya jata hai ar value hame
di jati hai.
 Myoglobin ka hill constant =1 and hemoglobin ka hill constant = 2.8 hota hai. Isliye
hemoglobin ke ander co-operative effect paya jata hai.

KULDEEP GARG CHEMISTRY (KDSIR) 67

Diagram of dissociation curve of myglobin

KULDEEP GARG CHEMISTRY (KDSIR) 68

 Ham dissociation curve of myoglobin and hemoglobin dekhen to hame ye pta chalta hai
ke approx 40mmHg partial pressure pe approx 97% saturation ho chuka hai oxygen ke
sath, jabki hemoglobin itne pressure pe sirf 50% saturate hota hai. Approx 100 mmHg
pressure pe jake hemoglobin aprrox 97% saturate hota hai oxygen ke sath.
 Agar partial pressure 60 mm Hg se 100 mm Hg (ΔP = 40 mmHg) ki baat kren to
hemoglobin ke saturation pe sirf 20% ka frk aaya. Ar 20 mmHg se 60 mmHg (ΔP = 40
mmHg) ki baat kren to hemoglobin ke saturation pe sirf 60% ka frk aaya. Kehne ka mtlb
ye hai ke jo oxygen ja rahi hai (body me ) wo 20-60 mmgHg pressure ki range me ja rahi
hai.
 Jab ham mountains pe jate hain to halki si problem hoti hai saans lene me pr zyada isliye
ni hoti hai kyun mountains pe jane pr pressure jo kam hota hai wo lungs ka pressure kam
hota hai , tissue ke pressure pe koi zyada frk ni padta. Ham Hb ka curve dekhen to jo
pressure me frk aaega wo saturation level(60 mm Hg - 100 mm Hg range) pe frk aaega ar
wo itna zyada ni hoga kyun sirf 20% frk hai. Maan lo uper mountains pe jake pressure 100
mmHg ki jagh 60 mmHg reh gya to kya hi frk pad gya usse, tissue pe to koi frk hi ni pada.
Tissue me jake to wo wahan se O2 uthaega. Jitni uthaega, wo 60mmHg pe jake wapis
utne percent saturate ho jaegi. KULDEEP GARG CHEMISTRY (KDSIR) 69
 Jo pressure difference ka frk padta hai wo lungs ke pressure pe padta hai na ki tissue ke
pressure pe.
Note:
To understand the whole concept written on previous slide see the recording from 28: 08
to 37:00
Note:
Ab explained concept se ek question banta hai.
Agar pressure kahin increase ya decrease ho to tissue pe negligible effect hota hai. Jo bhi
effect hota hai pressure ka, wo lungs pr hota hai.

KULDEEP GARG CHEMISTRY (KDSIR) 70

Ab yahan baat krenge blue shift and red shift ki (of hemoglobin Curve) (Trick)
Right Shift(means tissues ki trf shift) Left Shift (means lungs ki trf kab
shift hoga)
Tissue Lungs
Tissue me pressure Lungs me pressure zyada hota hai
kam hota hai (PO2 ) (PO2 )

pH pH
H+ H+
CO2 CO2
Temperature (jo bhi minor temp. Temperature
difference hota hai body ke tissues me and lungs me)

KULDEEP GARG CHEMISTRY (KDSIR) 71

Fraction nikalege

Mb + O2 MbO2
Kequlibrium = [ MbO2 ] Idher O2 ki concentration ni li jati balki partial
[ Mb]PO2 pressure liya jata hai because O2 ke sath ne ar bhi
gases jati hain to sari gases ke mila ke partial pressure
liya jata hai.

Mb + O2 MbO2 Suppose initially Mb ki quantity 1 hai ar MbO2 ki 0

1 0 hai to after time ‘t’ Mb ka fraction 1-f hoga ar MbO2
1-f f ka fraction f hoga.

fraction of MbO 2 f
K 
(1 - f) PO2 (1  f ) PO2

KULDEEP GARG CHEMISTRY (KDSIR) 72

 f f
K 
(1  f ) PO2 PO2  PO2 f

f  KPO2  KfPO2
KPO2  f  KfPO2
KPO2  f (1  KPO2 )
KPO2
f  Learn this formula for fraction of Mb
1  KPO2

 Exam me equilibrium constant de dega,partial pressure of O2 de dega ar fir Mb ka

fraction puchh lega. Ya graph bna ke de dega ya K and PO2 ki value de dega.
 Jahan 100% saturation ho raha hoga, wahan K (equlibrium constant) = 1 hoga. Ar jahan
saturation kam hoga, wahan product krke K (equlibrium constant) nikal lenge.
reactant

KULDEEP GARG CHEMISTRY (KDSIR) 73

Fraction of Hb

K ( PO2 ) n
f  Here, n = Hill Constant
1  K ( PO2 ) n

 Agar Hill Constant ki value ni de rakhi ho to n = 2.8 rakh denge for Hb.
 Hill constant Mb ke liye 1 hota hai. Isme dusre O2 ke aane se koi co-operativity ni badhti,
jabki Hb me me dusre O2 ke aane se co-operativity badhti hai.
Photosynthesis
Question 12:
6CO2 + 12H2O C6H12O6 + 6H2O + 6O2
1 2 a b c
Ye numbering (1,2,a,b,c) , oxygen ko di gyi hain. Ab batana ye hain ke a, b , c oxygen kis
kis (1,2) se bani hain.
(a) a 1, 2 (b) b 1, 2 (c) c 1, 2
KULDEEP GARG CHEMISTRY (KDSIR) 74
Ans: c oxygen (6O2) sirf 2 wali oxygen se bani hai i.e. sirf 12H2O wali oxygen se bani hai. a , b
wali oxygen sirf 1 wali oxygen se bani hain i.e. sirf 6CO2 wali oxygen se.
 Ar exam me question neeche diye gye question ki aaega.
Question 13:
CO2 + H2O18 ?
(a) C6H12O618 + O2 + H2O
(b) C6H12O6 + O218 + H2O18
(c) C6H12O6 + O218 + H2O
(d) C6H12O618 + O2 + H2O18
Ans: Correct option : (c)

 Photosynthesis ke 2 part hote hain isliye photosynthesis redox reaction hai.

6CO2 + 12H2O C6H12O6 + 6H2O + 6O2
 Yahan aisa ni hota hai ke reactant side me jo 12H2O hain unme se product side me 6H2O
nikal gye. KULDEEP GARG CHEMISTRY (KDSIR) 75
 6CO2 + 6H2O C6H12O6 + 6O2
 Ye uper wali koi reaction ni hoti. Aisa kabhi ni krna hai ke product side ar reactant side ke
6H2O kaat do balance krne ke chakkar me. Product side ke 6H2O reactant side ke CO2 se
aate hain na ki H2O se.
Photosynthesis
 Photosynthesis photochemical reaction to hoti hi hoti hai. Yahan photochemical energy
ko convert kiya jata hai chemical energy me ar chemical energy se banaya jata hai food.
 Photosynthesis ek redox reaction hai. Yahan ek jagh oxidation ar ek jagh reduction hota
hai.
Redox Reaction
Oxidation (P.S. II) Reduction (P.S. I)
H2O ka oxidation hota hai CO2 ka reduction hota hai
H2O convert hota hai O2 me CO2 convert hota hai [CH2O] me
H2O O2 CO2 [CH2O] (food)

KULDEEP GARG CHEMISTRY (KDSIR) 76

 Reduction wale part ko Photosystem I kehte hai ar oxidation wale part ko Photosystem II
kehte hain.
 Oxidation of H2O ko kehte hain splitting of H2O.
 Oxidation wale part me jab O2 tut ke nikal jati hai (oxidation potential ho jata hai), yahan
ka electron nikalta hai , ADP convert hota hai ATP ke ander ar NADPH jab ek electron leke
aage chalta hai to wo CO2 ko convert krta hai food me. { This is called splitting of H2O}.
 In the figure given below (next slide), H2O pe light ka reaction hua to wo convert ho gya
O2 me. Jab H2O convert hota hai O2 me to hame zarurat padti hai NADP+ ar ADP + Pi ki. YE
fir convert ho jate hai NADPH ar ATP me. Calvin cycle me CO2 enter krta hai ar fir ATP and
NADPH bhi enter krte hain, fir CO2 convert hota hai food me.
 Photosynthesis ki reaction green plants me hoti hai because unme chlorophyll hota hai.
Ar ye photosynthesis ki reaction cynobacteria me bhi hoti hai.

KULDEEP GARG CHEMISTRY (KDSIR) 77

 PS I and PS II wali photo

KULDEEP GARG CHEMISTRY (KDSIR) 78

Chlorophyll Ring
 In this ring, 6- membered rings are 4 and 5-membered rings are 5.

Chlorophyll ring photo

KULDEEP GARG CHEMISTRY (KDSIR) 79

 Phytin group photo

Functional groups present in chlorophyll a and b

Chlorophyll a Chlorophyll b
No IR peak for aldehyde group Characteristic IR peak for aldehyde group
Keto group present Keto group present
Ester group Ester group
Phytin group Phytin group
Aldehyde group

KULDEEP GARG CHEMISTRY (KDSIR) 80

 Photosynthesis

Photosystem I (PS I) Photosystem II (PS II)

KULDEEP GARG CHEMISTRY (KDSIR) 81

 BIO - INORGANIC
(LECTURE-5)
Photosynthesis
hν
6CO2 + 6H2O18 C6H12O6 + 6O218 (Balancing equation)
chlorophyll

 Ye wali sirf balancing equation hai.

 Koi ye bole ke LHS me O18 ka count 6 hai ar RHS me iska count 12 hai to ye kaisi equation
hui, to iska answer hai ke equation to yahi thk hai ar ye sirf balancing equation hai. Puri
reaction neeche di hui hai.
hν
6CO2 + 12H2O18 C6H12O6 + 6H2O + 6O218 (Actual equation)
chlorophyll
KULDEEP GARG CHEMISTRY (KDSIR) 82
 Ab issi photosynthesis wali equation ke do part hote hain :
Photosystem I Photosystem II

 Ab ham colour wheel dekhen to koi agar green colour dikha raha hai to wo red colour ko
absorb kr raha hoga.

Colour wheel ki photo VIBGYOR

Wavelength

Range of Red colour = 650 – 750

 Range of U.V. Visible = 300 – 750
 Ab isse ye cheez to clear hai hai ke photosystem 650 se uper ki range me kaam krega
kyun ke red colour ko absorb krega.
KULDEEP GARG CHEMISTRY (KDSIR) 83
 Photosynthesis sirf photochemical reaction ni hai . Ye Photochemical Redox Reaction hai.
Sirf photochemical reaction kehna, iska adhura naam hoga.
 Photochemical means photon ko leke reaction ho rahi hai. Yahan photon ko leke redox
reaction ho rahi hai.
 Yahan H2O ka oxidation hoga ar CO2 ka reducation hoga.

Photosystem II (PS II) Photosystem I (PS I)

H2O CO2
Oxidation Reduction
O2 Glucose (food)
[CH2O]

 PS I and PS II kis wavelength pe absorb krenge, uski trick. Jiske marks zyada aaenge wo
first ar ar jiske marks kam aaenge wo second hoga.
 Hence, PS I = 700 (PS I is also called P700)
PS II = 680 (PS II is also called P680)
KULDEEP GARG CHEMISTRY (KDSIR) 84
 Koi puchhne lage ke P680 ke ander kya hota hai to ham bolenge iske ander water ki
splitting hoti hai ar P700 ke ander recduction hoga and CO2 will convert into glucose.
 Exam me ye question bhi aa sakta hai ke konsi aisi reaction hai jo bina sunlight ke bhi ho
sakti hai , iska answer hai PS I.
 PS II (P680) ko ham Light Reaction bhi kehte hain because iske liye sunlight ki need hoti
hai. PS I (P700) ko ham dark reaction bhi kehte hain because iske liye sunlight ki need ni
hoti. Dark reaction ka mtlb yeni ke andhera kro tabi reaction hogi,iska mtlb hai ke bina
light ke bhi ye reaction ho jaegi. Agar PS I ko thermally kraenge to ye reaction thermally
bhi ho jaegi.
 PS II (P680) me ek complex aisa hota jo electron ke around kawach bna ke chalta hai ar
uska naam hai Mn4 complex. PS II (P680) se electron nikalta hai ar Mn4 complex uske uper
kawach bna ke chalta hai.
 PS II (P680) me ADP converts into ATP.

KULDEEP GARG CHEMISTRY (KDSIR) 85

PS I and PS II wali photo

KULDEEP GARG CHEMISTRY (KDSIR) 86

Route of electron
 Exam me puchha jata hai ke electron ka route kya hai. To usko learn krne ki trick hai.
Pehle queen ne Plassi ke yuddh me Bf (boyfriend) ke sath cyanide piya.
*
P680 Pheophytin Quinone Plastoquinone cytochrome bf
complex

P680 Plastocyanin

 Electron, P680 (PS II) se excited hoke excited energy me pahuncha ar fir yahan electron
Mn4 complex ke kawach me aaya. Fir yahan se electron jata hai Pheophytin ke pass. Uske
baad electron jata hai quinone ke pass. Quinone ek non- haeme protein hoti hai.
Quinone means Fe ke sath 2 groups lage hain.
Φ—Fe—Φ
 Plastocyanin ke baad electron jata hai P700 ke pass fir ye excite hota hai *P700 me. Iske
baad electron jata hai plant ferrodoxin (Fe2S2) ke pass. Ab yahan ek enzyme lagta
ferrodoxin reductase, iss enzyme ke pass electron jata hai. And then CO2 is coverted into
glucose. KULDEEP GARG CHEMISTRY (KDSIR) 87
 *
Plastocyanin P700 P700 Plant ferrodoxin (Fe2S2)

Glucose CO2 Ferrodoxin Reductase

(enzyme)
Reaction of Photosystem II (PS II) (Water Splitting Reaction)
2H2O + 2NADP+ + 2ADP + Pi O2 + NADPH + 2H+ 2ATP

Complete reaction of Photosynthesis

6CO2 + 12H2O C6H12O6 + 6O2 + 6H2O

KULDEEP GARG CHEMISTRY (KDSIR) 88

Nitrogen Fixation
 Ye plants me hota hai.
 Yahan N2 se NH3 banta hai ar fir ye NH3 fertilization me kaam aata hai.
Conversion of N2 to NH3 .
 Ab sochne ki baat ye hai ke ye ho kaise raha hai kyun triple bond se single bond me ja
rahe hain. Although ye clear hai ke NH3 zyada stable hai. N2 me triple bond (N≡N) hota
hai. Ar triple bond todne me kitni zyada energy chahiye .
 We know that
N≡N NH3 (Exothermic reaction) means heat release hogi

N2 to NH3 ka graph wali pic

KULDEEP GARG CHEMISTRY (KDSIR) 89

 Ye thik hai ke reaction exothermic hai but ye activation energy to bahot high hai.
 Nitrogen fixation 2 trh se hoti hai.
Nitrogen fixation
In vitro (outside the plant) In vivo (inside the plant)
Example: Haber’s Process
Haber’s Process Atmospheric conditions
N2 +3H2 NH3 N2 NH3

 Ham in vivo nitrogen fixation padhenge. Isme use honge nitrogenase enzyme, jo
atmospheric conditions me hi plant ke ander NH3 bna dete hain ar plant ke liye fertilizaer
ka kaam krte hain.
Types of Nitrogenase Enzymes
1. Vanadium Nitrogenase
2. Iron Nitrogenase
3. Molybdenum Nitrogenase
KULDEEP GARG CHEMISTRY (KDSIR) 90
 Suppose agar sirf nitrogenase likhr de ar koi specific naam na de to Molybdenum
nitrogenase consider krenge kyun sabse zyada yahi milta hai ar baki ke (Vanadium
nitrogenase and Iron nitrogenase) to bahot kam milte hain.
 Complete nitrogenase 2 cheezon se milke bna hota hai
1. P-cluster
2. M- Fe Co-factor (Metal –Iron co-factor)
 P-cluster to teeno trh ke nitrogenase me same hota hai. Difference aata hai metal- iron
co-factor me lage metal ka. Ab wo metal Vanadium ho skta hai, Iron ho sakta hai,
Molybdenum ho sakta hai, inhi metal ke basis pe nitrogenase enzyme 3 trh ke hote hai.

KULDEEP GARG CHEMISTRY (KDSIR) 91

Unit of P-cluster

Photo of P-Cluster

 Isme question ye puchhte hain ke P-cluster me konsi non-heme protein use hoti hai, to uska
answer hoga Fe4S4 .
 Ab isme puchh lega ke noitrogen fixation me jo non-heme protein hoti hai, usme kitne
inorganic S use hote hain ar kitne organic sulphur use hote hain..
KULDEEP GARG CHEMISTRY (KDSIR) 92
Unit of Co-factor

Photo of co- factor

 Ye jo yahan N≡N (N2) hai Mo se juda hai, isi ko convert krte hai NH3 me.
KULDEEP GARG CHEMISTRY (KDSIR) 93
Note:
Reaction of Molybdenum Nitrogenase
N2 + 8H+ + 8e– + 16MgATP 2NH3 + H2 + 16 ADP + 16Pi (inorganic phosphate)
 This reaction is for Molybdenum nitrogenase. Ar iss reaction me 8e– use hote hain and
8H+ use hote hain.
 Ab exam me nitrogenase krke puchhe ya molybdenum nitrogenase krke, answer issi
equation se dena hai.
 Iss reaction me hame ye yaad rakhna hai ke kitne electrons ar kitne H+ use ho rahe hain.
Ar ye bhi yaad rakhna hai ke kitne ATP consume hue ar kitne ADP bne.

Reaction of Vanadium Nitrogenase

N2 + 14H+ + 12e– + 40MgATP 2NH4+ + 3H2 + 40 ADP + 40Pi (inorganic phosphate)
 Vanadium nitrogenase me kitne electron use hote hain ar kitne H+ use hote hain to uska
answer ham iss equation se denge.

KULDEEP GARG CHEMISTRY (KDSIR) 94

 Ab baat aati hai ke kab molybdenum nitrogenase use hota hai ar kab vanadium
nitrogenase use hota hai. Iron nitrogenase to bahot hi na ke barabar use hota hai to isliye
hamne uski baat ni ki. Sabse zayda molybdenum nitrogenase milta hai, usse kam
vanadium nitrogenase ar sabse kam iron nitrogenase.
 Agar temperature, room temperature hai ya high hai to molybdenum nitrogenase kaam
karta hai. Agar zyada hi high temperature hai to zarurat hi hi ni hai, N2 khud hi convert ho
jaegi NH3 me, excitation energy leke.
 Agar koi plant aisa hai jo bahot hi low temperature pe hai to wahan Vanadium
nitrogenase. Low temperature pe molybdenum nitrogenase work ni krta to vanadium
nitrogenase use krte hain.

KULDEEP GARG CHEMISTRY (KDSIR) 95

Energy diagram

N2 Energy diagram ki photo

 Yahan 2 intermediates bante hain.

1. NH=NH
2. NH2—NH2
KULDEEP GARG CHEMISTRY (KDSIR) 96
Metal complex in medicine
Cis-Platin

Ye thoda ionic hota hai to Ye Pt jab DNA pe jata hai to Pt pe lage H2O
water ke ander jake jaldi break ho jate hain ar ye Pt DNA pe jake cis trf se jud
hydrolysis kr leta hai. jata hai.
Agar trans hota dono trf se bind ni kr pata

 Ye jo Pt attach hota hai DNA se , ye Guanine chain se attach hota hai.

 Ye jo Pt hai ye Guanine base se jake takrata hai ar cancer cells ka jo DNA hai usko tod deta
hai.
KULDEEP GARG CHEMISTRY (KDSIR) 97
 Ye hai Guanine ka structure ab Question me puchhta
hai ke guanine ke kis ‘N’ se jake judega Pt kyun isme 5
‘N’ hain.

 Ab yahan pe cis-platin aa raha hai to wo guanine ko marne hi to aa raha hai. In general

attack krna uspe easy hai jo akela hai rather than jahan 2 log ek sath hain. Sath me
chhota sa bachcha bhi chal raha hota hai to attack hone dr kam ho jata hai, isliye jinn ‘N’
pe ‘H’ hai unpe to attack hoga ni. Ab bache 2 ‘N’ * (b) and (c) +jo akele chal rahe hain. To
ab Pt ya to (b) se judega ya (c) se. Ab (b) and (c) me se dekhen to (c) wala ‘N’ alag sa pada
hua hai to attack issi pe hoga Pt ka.
 Pt guanine se (c) wali ‘N’ se judega.

KULDEEP GARG CHEMISTRY (KDSIR) 98

 Guanine me numbering aise krte hain to (c) wale N ki numbering 7 hogi. To guanine ke N-7 se
Pt judta hai.

 Cancer: Cancer means unwanted tissue.

Cis-Platin

 Cis-platin khane ke side effects bahot hain. Kidney kharab ho jati hai ar kidney damage hone ko
kehte hain Nephrotoxicity.
 Cis – platin khane se Neurotoxicity hoti hai, iska mtlb pura nervous system kharab kr deti hai.
 Ab inn dono toxicity se bachne ke liye ham ek aur platin lete hain. To aise cis- platin aage chal
kr convert hua carboplatin me.
KULDEEP GARG CHEMISTRY (KDSIR) 99
 Carboplatin ke side effects thode kam paaye gye ar ye dekha gya ke carbo-platin ovarian
cancer, lung cancer, head cancer me zyada effective paayi gyi.

 Carboplatin is less toxic than cis-platin.

 Cis-platin and carboplatin via injection di jati hain.
 Ab platin ka ek ar roop aaya jo orally diya ja sakta hai. Wo compound next silde pe banaya
huahai.

KULDEEP GARG CHEMISTRY (KDSIR) 100

 In this metal complex, Pt is in (IV) oxidation state.

 Iss lecture ki PDF me se ‘Possible modes of binding’ ki photo dekh kr jani hai hai, jisme
intrastrand cross linking and interstrand cross linking show kiya hua hia. (Lect. time:-
01:19:30 to 01:22:51)
 Experimentally intrastrand cross linking paayi gyi hai.

KULDEEP GARG CHEMISTRY (KDSIR) 101

 BIO - INORGANIC
(LECTURE-6)
(Revise India Gate 2021- 1)
 Hemoglobin, Myoglobin, Hemerythrin , Hemocyanin ka work oxygen se related hota hai.
 Hemoglobin and myoglobin vertebrates me milte hain.
 Hemerythrin and hemocyanin invertebrats me milte hain.
Hemoglobin

KULDEEP GARG CHEMISTRY (KDSIR) 102

 Hemoglobin ki 5th site judi hoti hai imidazole se (N ki side se).
 Hemoglobin ki 6th site O2 se bind hoti hai.
 Jab Fe porphyrin ring ke chaaron N se juda hai ar 5th site pe imidazole ke nitrogen se juda
hai to uska structure thoda pyramidal shape me hota hai ( plane se thoda sa utha hua ).

 Jab Fe, O2 se bind kr leta hai to porphyrin ring ke chaaron N ar Fe same plane me aa jate
hain.

KULDEEP GARG CHEMISTRY (KDSIR) 103

 Ab yahan se question uthta hai ke Fe se jab O2 ni juda tha to pyramidal jaisa shape tha.
Jab O2 jud gyi to shape planer ho gya. To ab ham baat krenge oxyhemoglobin ki ar
deoxyhemoglobin ki.
 Deoxyhemoglobin means abhi tak O2 ni juda hai ar oxyhemoglobin means jab O2 jud gya
hai.
 Ab question ye hai ke O2 judke ye structure planer kyun ho gya?
Iska concept ye hai ke jab koi cheez fasti ni hai to wo uper ki trf atki reh jati hai. Agar uss
cheez ka size chhota kr den to wo ring me fas jaegi. To jab Fe ke sath O2 juda tha ar jab O2
ni juda tha to Fe ke size me difference tha. Ar Fe me jo size ka difference hota hai, wo O.S.
ke basis pe hota hai.
 Jab Fe, O2 se ni juda hota hai (deoxyhemoglobin) to Fe ki oxidation state hoti hai +2. Jab
O2 jud jati hai Fe se to Fe ki oxidation state ho jati hai +3.
 +3 oxidation state me Fe ka size chhota hota hai ar Fe ka size chhota hone ke baad wo
planar structure bana leta hai porphyrin ring ke sath.

KULDEEP GARG CHEMISTRY (KDSIR) 104

Oxyhemoglobin Deoxyhemoglobin
It is relaxed state. It is tensed state kyun ke Fe koshish kr raha
ke ring me ander jaun pr ni ja paa raha hai.

Fe+3 Fe+2
Ab yahan +3 oxidation state hai Ab structure square pyramidal me chala gya
ar 5 jagh se N ki binding hai, to to spliting bhi yahan square pyramidal wali
ye low spin complex me convert lagti hai. To ye high spin complex hai.
ho jata hai. Binding achhe se ni ho rahi kyun ke
oxidation state kam hai.
Ek baat hamne co-ordination ki class me
padhi thi ke agar Fe ki binding N ki trf se ho
to Fe jab +3 oxidation state me hoga, tabi
low spin complex banaega, other wise high
spin complex banaega.
KULDEEP GARG CHEMISTRY (KDSIR) 105
 Oxyhemoglobin Deoxyhemoglobin
Magnetic nature : Diamagnetic Magnetic nature : Paramagnetic
(experimental hoti hai) (experimental hoti hai)
Super exchange mechanism ke
through ye diamagnetic hota hai.

Note :
Jab Fe ka bond ban jata hai oxygen ke sath to wo oxygen bent shape me aa jata hai.

Isska agar Raman Spectra len to approx 1100 cm–1 pe peak milti hai.

KULDEEP GARG CHEMISTRY (KDSIR) 106

 Ab baat aati hai ke jab hemoglobin itna sab kuchh tha to hame myogobin ki need kyun
hai.
Difference between hemoglobin and myoglobin
 Hemoglobin me aisi (jo right side
me show ki hui hai) 4 peptide chain
hoti hain. Inn 4 peptide chains ko mila
ke 1 hemoglobin banta hai.
 Jabki myoglobin me ye kewal monomer
hote hain.
 Agar molecular weight ki baat kren to
hemoglobin ka approx 64000 hota hai
(approximately 4 times the mol.wt.
of myoglobinar myoglobin ka lagbhag
16000 hota hai.
KULDEEP GARG CHEMISTRY (KDSIR) 107
 Suppose koi beemar hai to usse ambulance chhor ke aaegi hospital. Ab yahan ambulance
patient ko sirf idher se udher le jane ka kaam kregi, patients ko store ni ni kr sakti. Patient
ko rakhne ka kaam hospital karega. To iss example se samjhe to ambulance hemoglobin
hai ar hospital myoglobin hai. Hemoglobin, O2 carry krne ka kaam krta hai ar myoglobin
O2 ko store krne ka kaam krta hai.
 Jab ham saans lete hai to hemoglobin hamare lungs se O2 uthata hai ar deke aata hai
muscles ko ar muscles me present hota hai myoglobin.
 Ab koi kehne lage ke muscles me bhi hemoglobin ko present kr do, to aisa ni ho sakta.
Jaise koi insan ki kaam krne ki efficiency Kashmir me hai, wahi same efficiency uss insan ki
Kanyakumari me ni ho sakti.
 Hemoglobin ki jo achhi binding hoti hai O2 , wo hoti hai high pressure .

Isko co-operative
effect bola gya hai.
 Lungs ke ander O2 ka pressure zyada hota hai, jabki muscles me O2 ka pressure kam hota
hai. KULDEEP GARG CHEMISTRY (KDSIR) 108
 Myoglobin O2 ke sath low pressure pe best binding krta hai.
 Jaise jaise pH kam hota hai hemoglobin ki O2 ke sath binding decrease ho jati hai.
Low pH binding

Isko Bohr effect bola gya hai.

 Jab muscles ke pass O2 lekar jata hai hemoglobin to wahan blood me pH low hoti hai to
wo O2 ko myoglobin ko de deta hai.
 Next slide pe diye hue figure ko dekhenge to wo ye batata hai ke jo pressure O2 ka
tissues/muscles/blood me hai, uspe hemoglobin 50% hi saturate hota hai jabki same
pressure pe myoglobin 100% saturate ho jata hai. Hemoglobin ko 100% saturate hone ke
liye lungs wala pressure chahiye.

KULDEEP GARG CHEMISTRY (KDSIR) 109

KULDEEP GARG CHEMISTRY (KDSIR) 110
Cooperative Effect
 Hemoglobin me 4 unit hoti hain. Jab hemoglobin se first O2 judta hai to uske judne ke
rate ko ham constant K1 se represent kr sakte hai . Dusra O2 ar bhi fast judega with rate
constant K2 . Teesra O2 ar bhi fast judega with rate constant K3. Fourth O2 sabse fast
judega with rate constant K4 . Issi ko kehte hain cooperative effect.

K4 > K3 > K2 > K1 (This is cooperative effect)

 Cooperative effect ki baat hemoglobin me hi ki jati hai, myoglobin me ni because
myoglobin me to 1 hi unit hai.
Hemoglobin ki binding sabse better kiske sath hoti hai
 Oxygen ke comparison me hemoglobin ki binding CO ke sath 200 times greater hoti hai.
Yahi reason hai jab aaj lagti hai to aag se ni balki dhue se log zyada marte hain. Dhue me
CO release ho rahi hoti to ham O2 ki jagh CO ko inhale krna shuru kr dete hain kyun CO
binding bahot tezi se hoti hai.

KULDEEP GARG CHEMISTRY (KDSIR) 111

Hemerythrin
 Ye oxygen binding krta hai ( oxygen transport and storage).
 Hemerythrin me koi porphyrin ring ni hoti. Isme Fe se amino acids jude hue hain, kon konse
jude usse koi mtlb ni hai.

Isme jo ye beech ka OH group

hai, ye bidentate ligand ki trh
kaam krta hai mtlb μ-oxo ki trh
kaam krta hai. Yahan dono Fe ki
O.S. (II) hoti hai.

Colourless Pink/purple in colour (oxygenated form)112

KULDEEP GARG CHEMISTRY (KDSIR)
Isme left wale Fe ka co-ordination Yahan O2 right wale Fe se aake bind ho gyi.
already six hai ar right wale Fe ka Ar H ko as a bridging ligand bna denge. Isko
co-ordination number 5 hai. To O2 μ-hydroxo kehte hain.
jo aake bind hogi wo right wale Fe Yahan O2 judne se HO2– ban jata hai. Yahan
se bind hogi. dono Fe +3 O.S. me chale jate hai.

Raman spectra peak ≈ 850 cm–1

High spin state Low spin state
KULDEEP GARG CHEMISTRY (KDSIR) 113
Paramagnetic Antiferromagnetic
(due to super exchange mechanism)
Ek Fe ki spin ar dusre Fe ki spin to dono
Fe milke compound ko antoferromagnetic
bna denge.

ESR inactive

KULDEEP GARG CHEMISTRY (KDSIR) 114

Note:
 IIT-JAM me puchh leta hai ke hemoglobin me 5-membered rings kitni hai ar 6-membered
rings kitni hai.
 In hemoglobin
5 membered rings = 4
6 membered rings = 4

KULDEEP GARG CHEMISTRY (KDSIR) 115

 Students faste hain Vitamin B12 ke structure me.
Krun ke isme corrin ring hoti hai ar corrin ring me
ye red colour se represent kiya hua bond direct
hota hai.
5- membered ring = 5

Hemocyanin
 Jinn invertebrates me blue colour ka blood paya jata hai, ye unme present hota hai.
 Invertebrates me blue colour ka blood iski wajh se hi hota hai.
 Ye bhi oxygen bind krta hai pr iske bind krne ka tareeka alag hot hai . Abi tak jo padhe
hamne wo ek trf se bind kr rahe the but ye η(eta) me aakr bind krta hai. Isme O2 do
molecules ke beech me η form me judta hai.
KULDEEP GARG CHEMISTRY (KDSIR) 116
 Pehle O2 aise jud rahi thi.

 Ab hemocyanin me O2 aise jud rahi hai Cu

ke sath.

 Hemocyanin me deoxy form me Cu ki O.S.

+1 hoti hai. Ar jaise hi O2 judti hai to Cu (II)
O.S. me chala jata hai.
 Yahan hemocyanin me high spin and low spin
ka koi chakkar ni hai kyun ke Cu d9 /d10 me high
spin / low spin ka koi chakkar ni hota hai.
 Jab Fe hota hai, tab hi high spin and low spin ka
chakkar hota hai. KULDEEP GARG CHEMISTRY (KDSIR) 117
 Hemocyanin me blue colour ka reason hai LMCT (Ligand to Metal charge transfer). Here
ligand is oxygen(O2 )
 Hemocyanin me Cu+1 to colourless hota hai ar Cu+2 blue colour ka hota hai due to LMCT.
 Raman spectra peak of oxygenated form of hemocyanin ≈ 800 cm–1

KULDEEP GARG CHEMISTRY (KDSIR) 118

 Antiferromagnetic
ESR inactive

Diamagnetic

KULDEEP GARG CHEMISTRY (KDSIR) 119

Question 14:
Match the items given below in the three columns (NET DEC 2018)
Metallo protein Species coordinated Resonance Raman O—O
Metal Contrel(s) Stretching frequency
(cm–1)

A. Oxyhemoglobin I. η2 η2 - O22– X. 844

B. Oxyhemocyanin II. HO2– Y. 803
C. Oxyhemerythrin III. O2– Z. 1105

Correct matches
1. A-III-Z ; B-I-Y ; C-II-X 2. A-II-Y ; B-I-X ; C-III-Z
3. A—III-Y ; B-I-Z ; C-II-X 4.

Ans: Correct option : (1)

KULDEEP GARG CHEMISTRY (KDSIR) 120
Question 15: (NET DEC 2018)
Consider the following statements for the oxygenation of hemocyanine
(A) Oxidation state of both copper atoms changes by two
(B) It becomes intense blue from colourless
(C) Dioxygen is reduced to O22–
(D) The μ- η2 : η2 bond forms between each oxygen and copper atoms
The correct statements are
1. A and C 2. B and C 3. A,B and C 4. B, C, and D
Ans: Option (A) galat hai kyun ke copper atoms ki (+1) se (+2) me change hoti hai oxidation
state.
(B) , (C) and (D) are correct
Correct option : (4)

KULDEEP GARG CHEMISTRY (KDSIR) 121

Question 16:
The active site structure for oxy-hemerythrin is: (TIFR)/(NET)

KULDEEP GARG CHEMISTRY (KDSIR) 122

Question 17:
Consider the following statements for deoxy-hemerythrin and deoxy-hemocyanin:
A. They are involved in O2 transport in biological system (NET DEC 2018)
B. They contain two metal ions in the active site
C. Active site metal are bridged by amino acid residues
D. They prefer to bind only one O2 per active site
The correct statements are
1. A, B and D 2. A,C and D 3. B, C and D 4. A and C
Ans: Option (C) is wrong because hemerythrin se hi amino acids jude hote hain.
Correct option : (1)

Question 18:
The νO—O resonance Raman stretching frequency ( in cm-1 ) of the O2 co-ordinated to iron
centre in oxyhemoglobin is nearly:
(a) 1100 (b) 850 (c) 1550 (d) 1950
Ans: Correct option : (a)
KULDEEP GARG CHEMISTRY (KDSIR) 123
Question 19:
The O2 co-ordinated to metal ion in centres in oxy –myoglobin and oxy –hemocyanin exists ,
respectively as: (GATE 2018)
(a) Superoxide and peroxide (b) Superoxide and superoxide
(c) Peroxide and peroxide (d) Superoxide and oxygen
Ans: Correct option to baad me dekhenge pr hamko ye pta hai ke option (c) correct ni hoga.
Correct option : (a)

Question 20: (GATE 2016)

Durin oxygen transport hemeerythrin, oxygen is bound as
1. O2– to one Fe(III) only 2. HO2– to one Fe (III) only
3. O22– to one Fe(II) and one Fe(III) 4. O22–
Ans: Correct option : (2)

KULDEEP GARG CHEMISTRY (KDSIR) 124

Question 21: (GATE 2015)
Identify function hemocyanin and the metal responsible for it
1. O2 transport and Fe 2. O2 transport and Cu
3. Electron transport and Fe 4. Electron transprot and Cu
Ans: Correct option : (2)

Question 22: (GATE 2015)

Among the given pH values, the O2 binding efficiency of hemoglobin is maximum at
1. 6.8 2. 7.0 3. 7.2 4. 7.4
Ans: Jitna zyada pH badhega utni zyada binding badhegi.
Correct option : (4)

KULDEEP GARG CHEMISTRY (KDSIR) 125

Question 23: (GATE 2013)
Oxymyoglobin and oxyhemoglobin, respectively are:
(a) Paramagnetic and paramagnetic (b) Diamagnetic and diamagnetic
(c) Paramagnetic and diamagnetic (d) Diamagnetic andparamagnetic
Ans: Correct option : (a)

Question 24: (GATE 2012)

hemoglobin is an oxygen carrier protien. The correct statement about oxyhemoglobin is that:

(a) The metal is low-spin in +3 oxidation state while dioxygen is in O2– form.
(b) The metal is high-spin in +3 oxidation state while dioxygen is in O2 form.
(c) The metal is low-spin in +3 oxidation state while dioxygen is in neutral form.
(d) The metal is low-spin in +3 oxidation state while dioxygen is in neutral form.
Ans: Ab iss question me +2 oxidation to kahin bhi ni likhi.
Correct option : (a)
KULDEEP GARG CHEMISTRY (KDSIR) 126
Question 25: (GATE 2009)
In transformation from oxyhemoglobin to deoxyhemoglobin :
(a) Fe3+ in the low spin state changes to Fe2+ in the high spin state.
(b) Fe2+ in the low spin state changes to Fe3+ in the low spin state.
(c) Fe2+ in the high spin state changes to Fe2+ in the low spin state.
(d) Fe2+ in the high spin state changes to Fe3+ in the high spin state.
Ans: Correct option : (a)

Question 26: (GATE 2006)

Iron-sulphur cluster in biological systems are involved in
1. Proton transfer 2. Atom transfer
3. Group transfer 4. Electron transfer
Ans: Correct option : (4)

KULDEEP GARG CHEMISTRY (KDSIR) 127

 Summary Table
Hemoglobin Myoglobin Hemoerythrin Hemocyanin

Metal Fe Fe Fe Cu
deoxy +2 +2 +2 +1
O.S.
oxy +3 +3 +3 +2

Molecular 64000 16000 1,00,000 4 Lakh- 2 Cr.

Weight

deoxy Para Para Para Dia

Magnetic
Property
oxy Dia Dia Antiferro Antiferro
KULDEEP GARG CHEMISTRY (KDSIR) 128
 Hemoglobin ke red colour ki 2 peaks milti hai U.V. ke electronic spectra ke ander
Ek peak milti hai 400 nm pe ar dusre milti hai visible region me 450-750 nm

400 nm Isko SORET Band kehte hain

450-750 nm Isko Q- Band kehte hain
Inn Soret and Q-band ki wajh se ye π - π* transition ki wajh se intense red colour deta
hai.

KULDEEP GARG CHEMISTRY (KDSIR) 129

 BIO - INORGANIC
(LECTURE-7)
(Revise India Gate 2021- 2)
Electron Transfer Protein

Iron containing Copper containing

Iron containing proteins 2 types Iske under aati hai Blue copper protein
ki hoti hai.
Iske under aate hai:
Heme Non-heme 1. Plastocyanin Inn sab me
protein protein 2. Azurin Cu(II) me paya
Isme porphyrin Isme porphyrin ring 3. Ceruloplasmin jata hai
ring hoti hai ni hoti

Cytochrome Fe—S protein

KULDEEP GARG CHEMISTRY (KDSIR) 130
 Electron transfer kya hota hai, isse ham ek example se samjhte hain. Suppose kisi ek
organization ka chair person to uss tak ek letter jana hai to postman directly jake chair
person ko letter ni dega. Postman pehle jake watch man ko dega fir wo kisi ek box me
dalega fir uss box se ek clerk uthaega uss letter ko ar chairperson ke PA ko dega ar fir PA
jake wo letter chairperson ko dega.
 Watchman directly jake de sakta hai letter chairperson ko but dega ni. Yahin difference aa
jata hai oxidation potential ar reduction potential ka electron transfer system me. Kyun
hamko itne sare groups lagane padte hain cytochrome, haeme a, haeme b, haeme c,
kyuke inn sabka reduction potential alag alag hota hai. Isliye ek ke baad ek step pe
electron jata rahega ar electron transfer hota rahega.
 Jaise A se B pe 1 electron transfer hona hai to wo direct ni hoga , beech m cytochrome ki
help lete hain to wo A se electron leta hai ar fir B ko deta hai. To cytochrome ki do form
aati hai beech me, ek to reduced form jab electron accept krta hai ar ek oxidised form jab
electron de deta hai.

KULDEEP GARG CHEMISTRY (KDSIR) 131

Non- Heme Protein (Fe—S Protein)

 Agar S aise do metal se attached hota ar ham HCl se reaction krwate to H2S evolve hoti.

 Yahan 2 trh ke sulphur hain. Ek wo jo sirf 1 metal se juda hai, isse organic sulphur kehte
hain. Dusra wo jo do metal se attached (jo bridging me aa jata hai), isko inorganic sulphur
kehte hain.
 Inorganic sulphur HCl ke sath react krta hai jabki organic sulphur HCl ke sath react ni krta.
KULDEEP GARG CHEMISTRY (KDSIR) 132
 Non- heme protein is of 2 types:
1. Jo sirf Organic sulphur se bna ho.
2. Jo sirf inorganic sulphur se bna ho. Iss wale me organic sulphur bhi ho sakte hain pr
inorganic sulphur zarur honge.
Non –Heme Protein

Having only Organic Sulphur Having Inorganic Sulphur

(along with Organic Sulphur)
Isko ham Rubredoxin kehte hain Fe2S2 : Plant ferrodoxin

Rubredoxin ki oxidized state Fe(III)

hoti hai. Jab ye kisi se electron leta
to it will convert into Fe(II).

KULDEEP GARG CHEMISTRY (KDSIR) 133

Rubredoxin
 Isme jo Fe hota hai, wo 4 S (cystine) se juda hota hai.
 Isme ek bhi inorganic sulphur ni hai to ye HCl ke sath react ni krega.

Fe2S2 : Plant ferrodoxin

 Ye plant ke ander electron transfer ka kaam krte hain.
 Ham isko Fe2S2 likhte hain, isme S2 ka mtlb hai 2 inorganic sulphur.
 Isme ek question aata hai ke ye acid se react krega ke ni krega ar agar karega to kitne acid
molecules chahiye. To iska answer hoga ke ye acid react krega kyun ke 2 inorganic sulphur
present hain isme ar issiliye isko 2 acid molecues chahiye.
 Yahan jo 2 Fe present hai, unki apni oxidised state +3 hai. To ye anti-ferromagnetic
coupling show krte hain. Jiski wajh se inka ESR inactive hota hai.
KULDEEP GARG CHEMISTRY (KDSIR) 134
 Fe2S2 ko directly ham diamagnetic ni bol sakte kyun anti-ferromagnetism is a part of co-
operative mechanism. Isliye ham diamagnetic word use na krke ESR inactive word ka use
krte hain.
 Antiferromagnetic word ko ar diamagnetic word ko alag alag hi rakho because
temperature ka dono pe alag alag frk padta hai. Diamagnetic pe to temperature ka koi frk
ni padta.
 Fe2S2 only 1 electron krta hai.
 Jab Fe2S2 1 electron le leta hai to ek Fe +3 me hoga ar dusra Fe +2 me hoga.

KULDEEP GARG CHEMISTRY (KDSIR) 135

 Jahan sirf organic sulphur paaye jate hain, wo hote hain Rubredoxin ar jahan inorganic
sulphur paaye jate hain, wo hote hain ferrodoxin.

Ferrodoxin

KULDEEP GARG CHEMISTRY (KDSIR) 136

Question 27:
Iron – sulphur clustersin biological systems are involved in (GATE 2006)
(a) Proton transfer
(b) Atom transfer
(c) Group transfer
(d) Electron tranfer
Ans: Correct option : (d)

Question 28:
The number of inorganic sulphur (or sulphide) atoms present in the metalloprotein active
sites of rubredoxin, 2-2 iron ferrodoxin and 4-iron ferrodoxin, respectively, are:
(a) 0,2 and 4
(b) 2,4 and 3
(c) 0,4 and 2
(d) 0,2 and 3
KULDEEP GARG CHEMISTRY (KDSIR) 137
Ans: Correct option : (a)
2-2 iron ferrodoxin means Fe2S2
4 iron ferrodoxin means Fe4S4

Fe3S4
 Iski oxidized form me teeno Fe +3 O.S. me honge.
 Ye bhi 1 electro9n transfer system hai.

Fe+3 Fe+3 Fe+3

 Yahan super exchange mechanism bhi hogi ar antiferromagnetic coupling bhi hogi, tab
bhi yahan oxidized form ESR active rahegi because teeno Fe ke pass 5 unpaired electrons
honge each. Ab do Fe ke electrons couple kr lenge pr bache hue ek Fe ke 5 unpaired
electrons to reh hi jaenge.

KULDEEP GARG CHEMISTRY (KDSIR) 138

Fe4S4
 Isme 2 Fe +2 me hote hain ar 2 Fe +3 m3 hote hain.
 Isme oxidized form me 2 Fe+2 apas me antiferromagnetic coupling kr lenge ar 2 Fe+3 apas
me antiferromagnetic coupling kr lenge. To oxidized form ESR inactive ho jaege due to
antiferromagnetic coupling.

KULDEEP GARG CHEMISTRY (KDSIR) 139

 Abi tak hamne non-heme protein ke bare me padh liya ar ab baat krenge cytochrome
mtlb heme protein ke bare me padhenge, jo electron transfer krti hai.
Heme Protein
Ab baat krenge heme protein ki jo electron transfer krti
Cytochrome
 Ab baat aati hai difference between hemoglobin and cytochrome. In hemoglobin on 5th
site N(histidine) is attached and 6th site is vacant where as in cytochrome, on 5th site
N(histidine) is attached and on 6th site, sulphur containing methionine amino acid i.e.
S(methionine) is present.
 Cytochrome 3 types ka paya jata hai:
(i) Cytochrome a
(ii) Cytochrome b
(iii) Cytochrome c
 Inn sabhi cytochromes me sirf R1 and R2 ka farak hota hai. Ar issi ko kehte hain ke side
chain i.e. globin protein chain ka farak hota hai.
KULDEEP GARG CHEMISTRY (KDSIR) 140
Heme a Heme b Heme c

KULDEEP GARG CHEMISTRY (KDSIR) 141

 Heme a Heme b Heme c
R1 = C18H30OH R1 = R1 =
R2 = R2 =
R2 =

 Above given sabhi me porphyrin ring hoti hai. Fe ki 5th site

N (histidine) se judi hui hai ar 6th site, S (methionine) se
jud jati hai.
 Kai jagh galat bataya gya hai ke H2O juda hota hai. Pr
H2O isme ni balki cytochrome P450 me judta hai.
 Cytochrome P450 ek enzyme hai ar ye cytochrome a , b, c,
electron transfer system hain.
 Cytochrome me electron transfer hone ka tareeka ye hai ke electron sabse pehle
cytochrome b ke pass jata hai , cytochrome c ke pass ar fir cytochrome a ke pass jata hai.
KULDEEP GARG CHEMISTRY (KDSIR) 142
 Movement of electron from cytochrome b to c to a, ye reduction potential pe based hai.
Cytochrome b Cytochrome c Cytochrome c
Iska oxidation Iska reduction potential
potential zyda sabse zyada hota hai.
hota hai.
 Cytochrome b electron chhorta hai to electron cytochrome c ke pass jata hai ar fir ye
electron chhorta hai to wo cytochrome a ke pass jata hai. Fir cytochrome a se electron O2
ke pass jata hai.
Cytochrome b Cytochrome c Cytochrome c O2
 Ab baat aati hai ke O2 ko elelctron lene ki need padi hi kyun?
Hanme saans li to ab O2 wait kr raha hai ke me kaise bind karun Hb se, to ek electron tezi
se O2 ki trf bhaagega ar isse O2– (super oxo form) bna dega ar O2– bnte hi Hb iss pr
jhaptega. Yahi rason hai hame electron transfer ki zarurat padti hai. Jahan bhi electron ki
kami ho, wahan electron pahunche ar O2 ko bind karae.

KULDEEP GARG CHEMISTRY (KDSIR) 143

 Jaise hi ham saans lete hain ar O2 ander jati hai to use electron fenk ke mara jata hai ar O2
apne super oxo form [O2– ] me aata hai. Fir ye super oxo frm jakr ke metal se takrata hai
ar metal apna ek electron chhor kr ke bhaagta hai ar Fe+3 O.S. me aa kr ke O2– se bind kr
jaata hai. nAise electron ka circulation bna rehta hai.
Question 29:
Find νO—O of reactant and product:

(i) Reactant = Product

(ii) Reactant > Product
(iii) Reactant < Product
Ans: O2 B.O. = 2 O2– B.O. = 1.5
Agar bond order kam hota hai to stretching frequency bhi kam hoti hai.
Stretching frequency  Bond order Correct option : (ii)
KULDEEP GARG CHEMISTRY (KDSIR) 144
Note:
Bond order 3 2.5 2 1.5
No. of electrons 8 9 10 11 12 13 14 15 16 17
O2 O2–
 Inhi cheezon ka fayda uthata hai inhi ka ek enzyme i.e. Cytochrome P450. ‘P’ means
pigment and jo electronic transition hota hai, uski peak aati hai 450 pe, jiski wajh se isme
colour hota hai.
 Urine ke through wahi cheez bahr hoti hai jo water soluble hoti hai. Agar hamne koi
saturated food kha liya hai ar wo water me solublize ni ho raha hai to wahi hamari body
me fat ki trh jama hota jata hai. To water me soluble hone ke liye ham food ki polarity
badhate hain. Polarity badhane ke liye hamare pass ek hi cheez bachti hai i.e. O2 , food ko
oxidize ho kra sakte hain polarity badhane ke liye. Ar cytochrome P450 issi kaam me aata
hai, isko monooxygenase kehte hain. Suppose hamne saturated alkane (R—H) khayi , to
cytochrome P450 isko ek oxygen de deta hai ar oxyygen lete hi food polar ban jata hai ar
water soluble ban jata hai and urine ke through bahr ho jata hai.
 This means Cytochrome P450 hamari body ko detoxify krta hai. Ar ye kaam ye
cytochrome a, b, c ki help se krta hai.
KULDEEP GARG CHEMISTRY (KDSIR) 145
 Cytochrome a, b, c se electron transfer hota hai ar ussi ki wajh se R—H ka oxidation hota
hai.

 Cytochrome P450 ek hi oxygen deta hai isliye isko monooxygenase kehte hai.
 Ek baad yaad rakhe ki hai ke cytochrome a, b, c me sulphur methionine ka tha but
cytochrome P450 me sulphur cystine ka hai.
 Cytochrome P450 ki 6th site pe H2O juda hua hota hai.

KULDEEP GARG CHEMISTRY (KDSIR) 146

 Cytochrome a,b,c Cytochrome P450
5th site N(histidine) S (cystine)
6th site S(methionine) H2O

Cytochrome P450

KULDEEP GARG CHEMISTRY (KDSIR) 147

 The species after step 3 is actually :
 The species after step 4 is actually:

Cytochrome P450
KULDEEP GARG CHEMISTRY (KDSIR) 148
Iron Storage
Ferritin and Transferrin
 Ferritin hamare liver and bone marrow me paya jaat hai.
 Ab jo ham padhenge ye electron transfer kaa kaam ni hoga, ab hoga iron storage ka.
 Ab ham padhenge iron storage kaise hota hai ar hamari body me bacteria kyun ni lag
paate ar isme ferritin ka sabse bda role hota hai.
 Hamari body me RBCs hoti hai ar inka life span aprrox 120 days hota hai. To ye to
decompose ho jati hain ar Fe bach jata hai. Ar ye Fe sabki khurak hota hai.
Body me bacteria lag jaye to unko bhi chahiye hota hai Fe. Fe pe feed krke bacteria ar
panap jate hain.
Agar H2O ko Fe mil jaye to wo isko hydrate krke body se bahr nikal dega. To Fe ko water se
bacha ke rakhna hai.
 Ab Fe ko aise waste to ni hone de sakte to Fe ko ham store krte hain. Hamari body me ek
aisa house bna hua hai jahan koi Fe pe attack ni kr sakta, wo protein se ek dam dhaka hua
hai, ek cave like structure me. Wahan 4.5k Fe+3 jake store ho jate hain. Jaise hi body me
Fe ki kami hot hai to ek-ek krke Fe bind hokr jate hain wahan se.
KULDEEP GARG CHEMISTRY (KDSIR) 149
 Transferrin ka kaam hai Fe ka transport krna ar Ferritin ka kaam hai Fe ko store krna.
 Animals and humans me Ferritin paya jata hain.
 Fe +3 O.S. me store hota hai kyun ke Fe+2 ki binding kam hoti hai. Fe+2 apna ek electron
chhor deta hai ar Fe+3 me convert hoke Transferrin se bind ho jata hai fir wo usse ferritin
me chhhor deta hai.
 Ferritin me ek cavity hoti hai, iss cavity ke around protein apna jaal bichhae rakhta hai. Ar
protein iss hisab se apna jaal bichhata hai nke wo 2 layers bna deta hai. Ek bahr ki layer
hoti hai, jo hydrophilic and ander wala part jo hota hai wo hydrophobic hota hai.
 Hydrophilic part pehle to pass bulaega H2O ko ar fir usme se Fe leke ander rakh lega ar
H2O bhar hi fenk dega.
 Ar ye jo protein coats hain, ye 24 hote hain. Ar ek protein coat 175 amino acids se bna
hota hai. Isliye ek coat ke ander 4500 Fe+3 ko store kiya jata hai.
 Isme 2 channel hote hai:
(i) Hydrophilic channel
(ii) Hydrophobic channel
KULDEEP GARG CHEMISTRY (KDSIR) 150
 Fe+3 enter to krega hydrophilic channel se ar bahr niklega hydrophobic channel se.
 Transferrin 2 types ki hoti hai:
(i) Ova transferrin (ye ovum me milti hai)
(ii) Lacto transferrin (ye mother’s milk me hoti hai)
 Jab baby paida hota hai to usse mother’s milk diya jata hai sabse pehle taki baby me koi
bhi infection na ho. Lacto transferrin antibacterial agent ki trh kaam krt hai.
 Hamari body me bacteria ni lagte, isme ferritin and transferrin ka bahot bada role hota
hai.
 Microorganism me siderophores paaye jate hai jo iron transfer ka kaam krte hain. Hamari
body me bhi siderophores Fe le jake bacteria ko deta hai.
 Ek baat bahot achhi hai ke Fe+3 ke sath binding transferrin ki zyada achhi hai in
comparison to siderophores.
Transferrin > Siderophores (Fe+3 ke sath binding)
 Hota ye hai ke suppose bacteria hai ar uske pass iron hai pr transferrin ki binding bahot
achhi hai to transferrin apna Fe to dega ar bacteria ka Fe ki cheen kega usse. To bacteria
marna shuru ho jaega.
KULDEEP GARG CHEMISTRY (KDSIR) 151
 Yahi reason hai baby ko sabse pehle mother’s milk diya jata hai, jisse transferrin baby me
transfer ho ar Fe+3 ke sath binding increase ho ar wo bacteria ka bhi Fe kha jata hai.
 Isliye transferrin ko antibacterial bolte hain.
 Siderophore microorganisms me paya jata hai. Aisa ni hai ke hamari body me siderophore
ni paya jata hai, hamari body me bacteria hote hain to paya jata hai sideropore. Pr
siderophore hamari body me iron transport ka kaam kr ni sakta because hamari body me
usse better transferrin hai. Transferrrin ki binding bahot achhi hai.

Question 30:
The number of inorganic sulfides in cubane like ferredoxin and their removal method,
respectively, are (NET DEC 2017)
1. Eight and washing with an acid
2. For and washing with a base
3. Eight and washing with a base
4. Four and washing with an acid
Ans: Correct option : (4)
KULDEEP GARG CHEMISTRY (KDSIR) 152
Nitrogen Fixation
 Isme Mo and Fe metal use hoti hai.
 8 electrons ka use hota hai.
Vitamin B12
 Ye khoon ki kami ni hone deta hai i.e. anemia ni hone deta.
 Yaad rakhne wali baat hai iski 6th site.
6th site group Name of Vitamin B12
—CH3 Methyl cobalamin or Methyl Vitamin B12
—CN Cyano cobalamin
—OH Hydroxy cobalamin
—H2O Aqua cobalamin
—Adenosyl Vitamin B12 co-enzyme
 Agar puchha jaye ke Vitamin B12 ki 6th position pe konsa group laga hua hai to bolege
‘Adenosyl’
 Vitamin B12 me corrin ring present hoti hai na ki porphyrin ring.
KULDEEP GARG CHEMISTRY (KDSIR) 153
Vitamin B12GARG CHEMISTRY (KDSIR)
KULDEEP 154
The Na, K Pump or Na/K-ATPase
 Cell ke ander K+ zyada amount me paya jaata hai ar cell ke bahr Na+ ka amount zyada
hota hai.
 Jab inka cell ke ander-bahr exchange hota hai to 3 Na+ bahr se ander hain ar 2 K+ ander se
bahr jate hain.

KULDEEP GARG CHEMISTRY (KDSIR) 155