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BIOINORGANIC
CHEMISTRY
 Porphyrine Ring Heme Group/Fe-Porphyrine

A porphyrin is a large ring molecule consisting of

4 pyrroles, which are smaller rings made from 4
carbons and 1 nitrogen. These pyrrole molecules are
connected together through a series of single and
double bonds which forms the molecule into a large
ring Four 6 membered ring
Four 5 membered ring

11 pie bonds
Stable molecule
Considered to be aromatic
Hemoglobin

Porphyrine IX
Alpha chain- 141 amino acid
Heme b
Beta chain- 146 amino acid
Myoglobin

153 amino acid

Deoxy hemoglobin Oxy hemoglobin
Cooperativity
Effect
Physiology
Bohr’s Effect
Bonding And
Electronic
Structure of
Oxy
Hemoglobin
Bonding And
Electronic
Structure of
Oxy
Hemoglobin
Bonding And
Electronic
Structure of
Oxy
Hemoglobin
 Hematin
1. The Hydrocarbon Environment Round the Iron has a low dielectric constant and is
hydrophobic and therefore acts as nonpolar and provides non aquous environment.

2. It provides Steric hindranceand does not allow the formation of hematin.

 Hemerythrine
1.Non heme iron protein

2. Binds Oxygen Reversibly

3. Found in marine Invertibrates

4. In one molecule of hemerythrine there are 8 subunits and in each subunits there is
two Fe atoms.

5. No cooperativity effect Oxy hemerythrine

Both Fe Centers are Fe(III) Low Spin

Deoxy hemerythrine
Antiferromagnetic coupling
Both Fe Centers are Fe(II) High Spin
Diamagnetic

EPR inactive
Hemocyanin 1. Hemocyanin means BLUE BLOOD

2. Found in snails, squid, Crabs, lobsters etc.

3. Have several Subunits and Binds Oxygen Cooperatively

Deoxy hemocyanin

1.Bothe Cu Centers are Cu (I)

2. Diamagnetic
3. Colourless

Oxy hemocyanin
1. Blue in colour
2. Both Cu Centers are Cu(II)
3. antiferromagnetic coupling
4. diamagnetic
Cytochromes
Found in both plants and animals

Serve as electron carriers

Contain heme like prosthetic group

There are three main type of Cytochromes;

Cyt a, Cyt b, Cyt c

One electron carrier

Oxidised state is Fe (III) low spin

5th ligand is tightly bound S atom from

Methionine residue so no binding of O2.
Cytochrome c oxidase
Cytochrome P-450
Cytochrome P-450 are group of cytochromes found in Plants, animal and bacteria

Named as Pigment that absorbs at 450 nm with their CO complex

Functions as mono oxigenase

Structure
Contains heme group

Fe is present in Fe ( III ) state and is low spin Octahedral

One S- atom of Cysteine is Coordinated to Fe ( III )

Sixth coordination Site is occupied by H2O.

Reactions of
Cytochrome
P-450
 Catalytic
Cycle of
Cytochrome
P-450
 Iron- Sulphur Proteins

These are Non heme

Based on number of Fe
iron proteins and are
Contain one, two, four atoms divided in
responsible for
and eight Fe atoms. Ruberodoxin and
Electron transfer in
ferrodoxins.
plants and bacteria.
 Ruberodoxins
• Ruberodoxin is find In anaerobic bacteria
where it participates in biological redox
reactions

• Contains only one Fe atom

• Fe atoms is coordinated to four S atoms of

Cysteine in protein chain in tetrahedral
geometry

• Has no labile or inorganic sulfur

• Both Fe (II) ( reduced form ) and Fe (III) (

oxidised form ) are High spin in tetrahedral
geometry
Ferrodoxins
NHIP with more than one iron atoms are classified into three major categories
[2Fe-2S], [3Fe-4S] and [4Fe-4S] Ferredoxins

a) [2Fe-2S] or Fe2S2 Ferredoxin

Called plant ferredoxins

Contain two labile or inorganic sulfurs

One electron transfer agent

b) [3Fe-4S] or Fe3S4 ferrodoxin
C) [4Fe-4S] or Fe4S4 ferredoxin

Contains 4 labile sulfurs

Ntrogen fixation

Nitrogen fixation means conversion of atmospheric nitogen into ammonia

There are main two processes for nitrogen fixation

a) Biological process ( by bacteria )
b) Industrial Process ( Haber Process )

■Biological process by bacteria

The important bacteria which fix the nitrogen are Clostridium pasteurianum, Azotobacter vinerlandi and
Rhizobuim

■Nitrogenase enzymes: Nitrogenase are enzymes that are composed of two

metalloproteins; an Fe protein and the MFe protein

1. Vanadium Nitrogenase
2. Molybdenum nitrogenase
Molybdenum nitrogenase

Fe Protein or P-Cluster

Mo-Fe Protein nitrogenase ( active Site)

Iron Storage and Transport

Ferritin- iron storage

Transferrin- iron transport or scavanging

In Both Iron is in Fe (III) high spin

Siderophores
Siderophores are Iron containg complexes which are found in most microorganisms like bacteria and fungi

Also known as siderochromes because some of them are intensely coloured.

They are chelating ligands and form high spin Fe (III) complexes.

Complexes are stable but labile which allow the iron to be transported and transferred within the bacteria.

Some examples are : Ferrichrome, Enterobactine, Azobactin, Pyoverdine

Ferrichrome enterobactine azobactin pyoverdine

Photosynthesis Photosystems

Photosystem-I (P-700)

Absorbs light at 700 nm

Chlorophyll-
Responsible for conversion of CO2 into
glucose

Photosystem-II ( P-680 )

Absorbs light at 680 nm

Responsible for oxidation of water

Chlorin ring
Chlorophyll a

10 pie bonds
Mechanism
 Adenosyl cobalamin or Coenzyme B12
Vitamin B12 or Cobalamin R = 5’- deoxy adenosyl
Cobalamins are naturally occurring organometallic compounds
Cyanocobalamin is a manufactured form and other three are
naturally occurring forms of Vitamin B12

Cyanocobalamin
R = -CN

Hydroxycobalamin
R = -OH

Methylcobalamin
Corrin ring R = -Me

6 pie bonds
Cobalt is present in Co (+3) Low spin state
Diamagnetic and EPR inactive
Vitamin B12 contains cobalt in Co(+3 ) form and can be reduced to Co( +2 ) and Co(+1) form

Co(+2) complex = Vitamin B12S

and Co(+1) complex = Vitamin B12r

Co(+1) center in Vitamin B12Sis highly

Some reactions of Coenzyme B12
nucleophilic and can undergo following
reactions
CarboxyPeptidase - A
Catalyses the Hydrolysis of peptide bonds in the process of digestion

Structure of Active Centre

Mechanism
Carbonic anhydrase

Structure
Mechanism