Scribd Logo
Upload

Welcome to Scribd!

  • A K Das Bio-Inorganic Chemistry

    Uploaded by

    Sinduja
    4K views203 pages

    Copyright

    © © All Rights Reserved

    Available Formats

    PDF or read online from Scribd

    Did you find this document useful?

    Is this content inappropriate?

    Report this Document

    Copyright:

    © All Rights Reserved
    Download as PDF or read online from Scribd
    Flag for inappropriate content
    4K views203 pages

    A K Das Bio-Inorganic Chemistry

    Uploaded by

    Sinduja

    Copyright:

    © All Rights Reserved
    Download as PDF or read online from Scribd
    Flag for inappropriate content
    of 203
    BIOINORGANIC CHEMISTRY Asim K. Das Chapter 1 1 12 13 14 15 16 WwW 18 + Bloclements, Biomolecules and Background Materials Essential and Trace Elements and Bioinorganic Chemistry. Periodic Survey of Essent ial and Trace Elements : Biological Importance and Relative At \undance of the Elements. ‘The Cell and Distribution of the Elements in the Cell, Biomolecules : Background Materials : sugars; organic acids; amino acids, peptides and proteins; enzymes; purine and pyrimidine bases, nucleosides, nucleotides and nucleic acids; NAD", NADP+, FAD, FMN and quinones; lipids and phospholipids. Bicligands in Biocoordirfation Chemistry. Biological Fun: 's of Biometals (Summary), Chemistry of Physiological Butters. Probable Mecrianism of Carcinogenesis and Mutagenesis by Some Chemical Coniounds and Physical Agents like lonising Radiation Exercise Chapter 2 : Metal-Protein Interaction : Metalloenzymes : Role of Metal tons in Biological Functions 2.1 Metal-Protein Interaction : Metalloproteins and Metal-Protein Complexes 2.2 Metalloenzymes and Metal-Activated Enzymes, 2.3 The Role of Metal fons in Melal-Protein Systems : structural ynthesis of macrocyclic bioligands; blocking of Lewis acid catalysis in metalloenzymes; biological redox reactions; electron transport process. 2.4 The Role of Metal Ions in Basic Biological Reactions, 2.5 Binding of Transition Metal Complexes with DNA as Nucleic Acid Structural Probes : different conformations of ONA, general features of DNA-metal complex interaction, enantioselective interaction. Exercise 0 1-33 34-58 Chapter Blochemistry of Some Important Blometals, Storage, a ‘Transport and Activity 59.5, $1 Blochemistty of Iron and Iron-Metabolism : differant Fe-containi Proteins and enzymes and structural features of different Fe-proteing; ribonucleotide reductase (RR) ang methane epeoxygenase (MMO); transport and storage in higher animals and lower organisms. 3.2 Biochemistry of Copper and Copper-Metabilism ; different Cu- Containing proteins and enzymes and their structural features; transport and storage of copper; microbial mining of copper, 33 Similarities between Copper and Iron in Biological Proces: 34° Biochemistry of Zine : different 2n-containing enzymes; chemistry behind nature's selection of Zn(l) in enzymatic activity; binding Stes of Znil) in proteins - catalytic and stroctures sites, 35° Vanadium, Chromium, Manganese, Cobalt, Molybdenum, Tungsten and Nickel in Biology, $6 Transport and Storage of the Metals other than Iron, 3.7 Biochemistry of Calcium : Biological roles of calcium; binding sites of Ca? in proteins; storage of calcium; calmodulin (Ca? ion Carrion) Ga?*in muscle contraction; Ca? in blood Clotting process, 38 Comparison of Biochemistry of Ca?+ and Mg?*; Selectivity of Caz over Mg? in Biochemical Processes, Exercise Chapier 4 ; Transport Across the Membrane fon Pump lonophore 96-117 41 Active and Passive ‘Transport Across the Membrane, 42 ton Transport, 43° Crown Ethers and Cryptands ‘44° Naturally Occurring lonophores : Naturally Occurring Antibiotics ~ diferent types; mechanism of ion transport; valinomycin; Nonactin; gramicidin, 45° Models of Active Transport of Cations Across the Biological Membrane through the lonophores. 46 Sodium-Potassium Pump and Na*-K*-ATP-ase, 47 Active Transport of Na* and K+ ‘ons and Nerve Impulse : Na* -and K+-channels, 48 Calcium Pump and Ca*-ATP-age 49° Cotransnt of Sugars and Amino ‘Acids Driven by Na*-Flow. Exercise Chapter 5 ; Onygen Transport and Oxygen Uptake Proteins 118-154 2): thermodynamic and kinetic aspects of activation of dioxygen through metal ions, ay 5.2 Basic Requirements of Etfective Oxygen Carriers, 5.3 Biological Oxygen Carriers. 5.4 Distribution of Oxygen Carrying Proteins in Biological System. 5.5 Hemoglobin (Hb) and Myoglobin (Mb) in Oxygen Transport Mechanism : structural features of Hb and Mb; function of Hb and Mb; characteristics of O,-binding interaction with Hb and Mb — Cooperativty, Hill-plot, allosteric effect; effect of Ht, Clr, CO, and 2,3-ciphosphoglycerate (DPG); mechanism of homotropic and heterotropic allosteric ‘effect; protection of heme {rom its irreversible oxidation by O,; model systems; role of distal and proximal histidine; function of globin protein; nature of Hb-O, binding: Poisioning towards Hb and Mb. 5.6 The Role ot Hemoglobin in Acid-B: Balance and Carbon Dioxide 5.7 Hemarythrin (Hr) — An Oxygen Uptake Motalloprotein, 5.8 Hemocyanin (Hc) — An Oxygen Uptake Metalloprotein. 5.9 Synthetic Oxygen Carriers : Coliman's compound; Vaska's complex; cobalt(ll)-schiff base complexes; pertiuorochemicals (PFCs), 5.10 Hazards with Dioxygen in Biological System. Exercise Chapter 6 : Metal-containing Enzymes in Hydrolysis, Decarboxylation and Group Transfer Reactions : Lewis Acidity of the Metal lons 155-175 61 Peptide Hydrolysis and Peptidases, 62 Carboxypeptidase A (CPA) — Structure and Reactivity. 6.3 Thermolysin — Structure and Reactivity. 64 Leucine Aminopeptidase — Structure and Reactivity. 65 Mode! Complexes of Peptidase Reactivity. 6.6 Adenosine Deaminase (ADA) and Cytidine Deaminase (CDA) — Structure and Reactivity. 6.7 Arginase — Structure and Reactivity. 6.8 —_Urease — Structure and Reactivity. 6.9 Alkaline Phosphatase — Structure and Reactivity. 6.10 Purple Acid Phosphatase (PAP) — Structure and Reactivity. 6.11 Insulin Structure and Reactivity. 6.12 Hexokinase in Phosphorylation of Glucose and Enzymatic Reactivity of Some other Representative Kinase Enzymos. am 6.13 Carbonic Anhydrase (CA) — Structure and Reactivity, 6.14 DNA Polymerase — Structure and Reactivity. 818 — Carboxylaso and Docarboxylaso — Structure and Reactivity, Exercise Chapter 7 + Metal lons in Electron Transport Proteins and Redox Enzymes 176-235 7.1 Franck-Condon Principle and Designing of Electron Transport Agente in Biological System, 7.2 Won-Sulur Proteins : gonoral featuros; rubredoxin (Fd); ferredoxins (Fd) ~ 2F@-28, Riesko contros, 4F 0-48, high potential iron proteins (HIP), 3Fe-48, 8Fe-8S; Fe-S model compounds; nonredox Fe-S Protein, 7.9 Blue Copper Proteins : electron transport proteins and oxidase Proteins ~ laccase, ceruloplasmin and ascorbic acid oxidase (AA), 74 Nonblue Copper Oxidase Proteins : galactose oxidase (GO) and ‘amine oxidase. 78 —_Cytochromes : structural features and classification; cytochrom 7.8 Cytochrome c oxidase ~ Structure and Reactivity 7.7 Cytochrome P-450 ~ Structure and Reactivity, 7-8 Suporoxide Dismutase (SOD) — Structure and Roactvity 79 Catalase and Peroxidase — Structure and Reactivity. 7.10 Comparison of the Mechanisms of Action of Catalase, Peroxidase and Cytochrome P-450. 7-41 Oxygenases and Hydroxylases ; dioxygenases and mono- Sx¥genase; catochal-1,2-dioxygenase (CTD) and protocatechuate. ‘scervomnpee (PCD); tyrosinase; methane monooxygenase (MMO). 7.12 Alcohol Dehydrogen: + Liver Alcohol Dehydrogenase (LADH) 7-13, Molybdenum Containing Redox Enzymes : structural features and mechaniam of oxo-transfer activity; xanthine oxidase, suite end Oxidase; nitrate raductase; formate dehydrogenase (FDH); aldehyde oxid 7.14 Tungsten Containing Redox Enzymes — Some Representative Examples; Chemistry of Tungstoenzymes vs. Molybdoenzymes. 7.15 Some Important Organic Redox Couples. Exercise (iv) Enzyme Catalysed Hydrogen Production 236-275 8.1 Oxidative Phosphorylation and Respiratory Chain: elactron carrors in toepiratory chain; respiratory chain and synthesis of ATP; Cnergetics of the process and detection of ATP gonarating sites: blocking of respiratory chain, 5.2 Nitrogen Fixation : thermodynamic and kinalic aspects; dintrogen Complexes and activation of dinitrogen, $3 Nitrogenase (Ny-a8e) in Biological Nitrogen (N,) Fixation : occurrence; composition of the enzyme; structural aspects; model different types of substrates active towards nitrogenase; function Glfforent units in the activity of N,-a80; possible reaction pathway of reduction of N,. Ablological Nitrogen Fixation through Complexation. Photosynthesis and Chlorophyll : reaction; light phase and dark Phase reactions; chlorophyll - structural fontures; role of Mg(ll); electron transport chain (Z-scheme); oxygen evolving complex (QEC); antenna chlorophyll and reaction centro. %6 —Hydrogenase : biological significance; molecular properties of dihydrogen; composition of hydrogonase enzyme; hydrogenase Calatysed H,-proguction — a source of energy. 87 Carbon Monoxide Dehydrogenase (CODH) and Acetyl CoA Synthase (ACS). Exercise Chapter 9 = Phosphate Group Transfer and Metabolic Energy 276-304 ot Phosphate Transter : A Source of Metabolic Energy — ‘thermodyamic and kinetic aspects. 9.2 Phosphatases : General Mechanistic Aspects of Phosphate Group Transfer and Hydrolysis — studies on model complaxes, 9.3 Mechanism of Hydrolysis of ATP and Phosphate Group Tran from ATP : ATP-ase and Kinase Enzymes. 9.4 — Role of Phosphate in Glucose Metabolism : Glycolysis; tate of Pyruvate; citric acid cycle; glycogen synthe: Exercise Sbapter 10 : Vitamin B,,, Vitamin B, and Coenzymes 305-323 10.1. Vitamin By, and Coenzymes : structural feature; names of differant forms; chemistry of cobalamin; biochemical functions of cobalamins; models of vitamin B,,; special characteriatics of B,, coenzyme ) 10.2 Metnaneagenic Bactona Factor (F-430 M), 103 Vitamin 8, and Coanzymes : in the activity of transamination, cxidative deamination, decarboxylation and racomisation ot arming Acids; amino oxidase; lysyl oxidase, Exercise Chapter 11: Biochemistry of Nonmetals 324.33, 11.1 Biochemistry of nonmetals. 11.2 Nonmatals in Structural Uses : Examples of Biominoralisation, 11.3 Biological Rolo of Some Trace Nonmetals - boron; silicon: sultur: ‘selenium: arsenic ; fluorine; chlorine; bromine: iodine. 11.4 Biological Importance of Nitric Oxide (NO) Exercise Chapter 12 Metals and Chelation in Medicine 337-409 ‘12.1 Dependence of Biological Growth on the Concentration af Essential and Toxic Motals. 122 Disease duo to Moial Deficiency and its Treatment : Fe-, Zn-, Cu, Mo- deticiancy and treatment, 129° Motal ton Toxicity : sources of toxicity; goneral aspacis of mechanism of toxicity: importance of biomathytation in metal lon toxicology: chemical speciation of some metais in environments, 124 Toxic Elects of Matals : Fetoxicity; Custonicity and Witson's disease: As-toxicity, Hg-toxicity; Pbstoxlclty; Cd-toxicity; Al-toxicity: Ca-tonscity: toxicity of other motals: radionuclide toxicity: metnis ne carcinogens. 12.5 Natural Detoxilication of Metal lon induced Toxicity and Cleanup of Toxic Metals by Plants, 12.6 Required Thermodynamic and Pharmacokinetic Properties of Chelating Drugs in Metal lon Detoxification. 12.7 Soma Representative Chelating Drugs used in Metal ion Detoxification : —SH group containing drugs: polyaming- ‘carboxylates; dosterrioxaminss; aurinetricarboxylic acid otc, 12.8 Limitations of Chelation Therapy in Matal lon Detoxification. 12.98 Radioprotective Chelating Drugs and Therapautic Activities of Some Special Chelating Agents by Inhibiting the Metalloanzymes, 12.10 Matal-Metal Detoxification : Antagonism and Synergism among the Essential Trace Elements. Anitimicrobial Activities of Metal Chelates and Cheiating Ligands ; ionophore antibiotics; totracyclines; oxines; bleomycin; ‘As-, Sb- and Hg-compounds, ete, (vi) wi 1213 wa 1248 12.16 207 128 1200 Metal Chelation and the Activity of the Multipurpose Drug, Aspen, Mercunais as Ovuretics Antantwrtic Gold Drugs and Chrysotherapy. Antieftammatory Effects of Zinc and Copper Compounds. Ze Sak in the Treatment of Sickle Cell Anemia Lamum Therapy in Psychiatric Mind Disorder. 12.20 Anticancer Activity of Some Other Metal Complexes. 22 Radioisotopes in Medicines. 12.22 Bamuth Compounds in Medicines. 1223 Vanadium a Insulin Mimetic Agents in the Treatment of Diabetes. 1224 Mics of Superoxide Dismutase (SOD) Enzymes as Therapeutic Agents in the Treatment of Oxidative Stress. induced Diseases ~ Synzymes. 1228 Chelation and Role of Metal Complexes in Conventional Orug Resistant Malaria 1228 Metais and Chelation in Medicine — Summary Exercise Bibbography References (consulted) & Acknowledgement (wi) 12 O-Cry Bioelements, Biomolecules and Background Materials 1,1 ESSENTIAL AND TRACE ELEMENTS AND BIOINORGANIC CHEMISTRY The presence of about 40 different elements has been established in living bodies. The eleven most abundant elements in biological systems are H, O, C, N, Na, K, Ca, Mg, P, S, and Cl ‘Among these, the first four elements, |.e. H, O, C and N, constitute about 99% of the total ‘atoms of a living body. These elements are involved to produce the biomolecules like water, carbohydrate, protein and fat The next eight most abundant elements are Mo, Mn, Fe, Co, (Cu, Zn, F and |, These eight elements are present at trace quantities. These elements are called essential trace elements but the term trace Is not well defined, For example, Fe is present in few g ‘while Mo is present in few mg in an adult healthy body, but both are called trace elements. In fact, in ‘this group, except for F (ca. 2.6 g per 70 kg body weight in human being) Fe and Zn, all other ‘essential trace elements are present in mg scale in a living body. The next eight important elements ore Li, Si, V, Cr, Se, Br, Sn and W. These elements are required at ultratrace concentrations (|.¢. at the level of parts per ten thousand million). The biometals are classified as essential metals and beneficial metals. In the absence of tial metals, the living system cannot survive and it eventually dies. On the other hand, in the ince of beneficial metals, the life process gets hampered but it cannot lead to death Essential metals : Na, K, Mg, Ca, Mn, Fe, Co, Cu, Zn, Mo. Beneficial metals : Li, V, Cr, Ni, Sn, W. ‘The approximate metal contents in a healthy human body (ca. 70 kg body weight) are as follows Na (100 g), K (200 g), Mg (35 g), Ca (1500 g), V (15 mg), Cr (2 mg), Mn (15 mg), Fe (5-7 g), Co {1.5 mg), Ni (S mq), Cu (200-300 mg), 2n (2-3 g), Mo (10 mg). The amount indicated does not measure the importance of the metal. The decreasing abundance of the transition metals in living organisms is: Fe, Zn, Cu, Mo, Cr, Vand Ni, The total metal content shown here accounts for only ca, 2% of the total body weight. Excluding the metals Na, K, Mg and Ga, other metals ‘collectively weigh just a few grams (ca. 10 g) in a healthy body of ca. 70 kg. But these metals are extremely essential for the survival of life process 4 At biological pH, all these biometals (except for Na, K, and Ca to ‘CONMO exist as free ions, They should form insoluble hydroxides and phosphates. By bioligands. these biometals form soluble complexes 00) ara, oor i hr ma ar Ch ‘Sone "Alt en som saan rete ua Fe or ens bt ew wate 1Sdots eran sh se sensor of yn eso ad he emergence ‘Shenors,TieFeS00 sa SOD ae she ty ese he atl tn (Selo Dna Or he sts ht CoZn S00 ey se a oes nt rae Se upd core "Than C2 0 wa mh eer seve ee Op 1.3.1 CHLL AND DISTRRUTION OF THE HEMENTS In THE CL sey nh tale cl Twp cl nd oa ae ia ‘rea ramoce eb moore hove! hehe opr we ‘ela eon ofp oh i ser gon x proce 9 mane Sten rome hoger or hs by 8 aes Fld Morte ‘nes. Tey mani ges apo Ucar to sce ‘ro ath cnareten er tre mbar Se. Fier 141.: tana Sv ted sr Dd Fey ewe 143 oma a eda a arma inert a ee ne Sear ane Sura eee See Sao ‘Swecrmers chm tn el i ese eae elastin nay caring ety amin ad MACHINED nt eta oi a 2 eee rerienctery (ese Moca cu oncin nec are se og re graton Teele st aon pan nou owe daca et Sl Pi 1 Sa ned Aer 45 onda ioe ae ‘epshep hr rae e ee wis ths papa ‘ie mete oi mo pono ihe ge 10500 te Te at totum ns pny de. etre me Pay cet teh a te ee Sct smc fe tin Th pl rene sbi eile selec tose ag tar Se pr da ag rece Tas ret conn ne tom wach nein ee re it oye meio eect cea a a all [oie s tram cong tere bec ea 4482 jonencarve creas ee ep ny et nae rc ne toa lang ecb Meena) cere nay ged rh te fami, of ie el dave Te 5 nkage formed om Be fre) (ee on bf See 113 earner ore ses 414 jmodforcae ounemn ge 1438: Dagomacnpmratonl pen ce Cceternry ttre of the protein Sr stn of man pes ae a ty che fn coir bonis Toe may ance lon lve et Tats, Heegae conecs to steht ec To he epee pet en earnrine, Ten (Ses dejensine soma th es power. 9 ued The bon gr “Sie ertemary strectore of DNA gues the seqsence af eoxsritoniciotes it Sie ec ease rts mi ee Aad tpsther about hr nan sn rey be noted it hereon Po pon Bontng sed iy 1091) m te stant one epee chan he ‘honed tno DN se! ty Fong recon bnew te DMA aes SSSR stat ek eying ston Feb ntactor LABS EE 1a30) eee wh franc AT od gure nth cron 6.) Tem ‘Shee neces eieen he computa sn con econ “The por gps ie mes ce nd phorphaet baton me ee sarong sqaure sow harper On bee ad, (elope a Sees eed at nc 2 hve sed om Tpotuce beth ydrphoncintreton aed Mending sees fe dcton of at nae nce of DN, Teasend Ge 251" Ty cnt el oat mosis wh $B Be 4m jmonorcanse ewan nt ee permease nti Speeisarpnove eactan heswerni osama th el aereaeeetonn ea tees tns ene a eset fsa ae MN Se Bon Prt as prose cena san nF 1458 ] a i k i e488: Stent opto pee yes ule one pn eget {relent ete cdg ONA sa Lee be roeg DA tan ep at fA 27H {ADH Fatt — Necron Cavers the tne BAD" cade ik ee i ae otc cces ore Slrroienamen coon Be downs te, on” Moin) Shee 1484: foe 00M, ‘reg eer gine tien eis nell open Ta sand sho ond corse, Te ote dat ec hk Iepriei tl The nar fire res me opt The oa {erm mma yen ota tu pron mtn ded es Ge | hettoy sous mal rad he ney by ben nino ‘esegon 6 Fa 8.11 taheh send phones Betoun Be ergata ng wih nd Te soos oust mie erento a eo Agni meine, sa can cmon oma ta Sth mateg tooo pene, MGS Ca ATPase the est potee herman eons osha, Me gid sitet, ATP cn, gate up tame. Regd a ne nance fcr OT) neo meta: ee oe octal ceed man yo GAM f on Sree oe magyisir.Toare TERI bene ten Sacer en repr et on | O/C FDS Sa cps ceteris SP RSE cs apie nr wr Se cp ero tn nr Te SAID rn ec! oms GSES tegen i mr yd HO, wh he Se Ta oso “eager Z 1 ein se te tn rn FCO Frere aoe peraanes Silber aoc (62 Ny aon 7 Hea reeonis a HOO, + erst ‘Man hen = 74 eto COSCO, wm ra ~ 7st ob St enn $400; 11C04 20 on C0, peat om, Integy whe on H*onts prminy eoonng acton e orb N00; = oe oH, 1400, == 0 +0, (nse, CAs Hise ct th fo Ht ad creo of on no agi SS amt, any a ey ek thnainiaten se ice ‘Weatge Sf soon se. The “Ot fe rc! ms Hato 0 pede | heh urn reco the pear oxen to prefs the poral ad (Sipotna Toe pecomted an oor soe se. The mck “OH (LET chen iar arminton ate C8 come ef anne and sere ‘ncxporaion creak De icbnwee ‘Metal-Protein Interaction : Metalloenzy! Role of Metal lons in Biological Functions 12.) METAL-PROTEIN INTERACTION : METALLOPROTEINS [AND METAL PROTEIN COMPLEXES mene ceo ce ve ted mateo sh, Tha, pent tins es an 31h ccarna tals prio ey roe he Pesreeti eat eto! (00.0 ane (NP), so (OF, ol (8, Bezongta te Thee hnctoal ip con parpatem competion with te mat ‘Bed obese fra rrr, he met cen ae os Des ne Sa eElotcrcs cing mctaloenya sd metloctoted Prot dae combice Ing meactted errs) Ba tere 70 shay Feet ere se gx nce of he cium onset the metal ro itercon fy are aunt cides + apoprcten =" talon en 1 vey ine, the teraction leno mtllopten and Krai sa lene 9 metalctated pron Malloprotclns Here the rt oe 50h bln ith te poten ta te me can enegedaloran inter part ofthe protein srctre Insc cs, the tlio ca peers creme chem arch. The tains ery mach speci ch ‘The acoty of te mop tf be cncrnd etl renove Metabacthated Precis: sich os, tert en roves combined wt he ed hepealincan remain sxe of te meta, he poten ac | Gite opin echccl by wean che mol on Srctnes, herve metal ‘rely ter rl ir roe ects Ths, bow eter 1 (Goraraonenirnmn! oft oe on sedate met on Bolg cts, Compostion ofthe mata proten stem: For alloprotins ard metalleneymes. ata rcs roti esata 2 cosas sal stb puyol he seen scene finaly acer tw contat vale wher the stm bn 9 pure sate Ths ro ges etlotic ni lta ten inthe make The molar rao of meta to proton ‘oe of protein conta one leo 20 an ae aon ss vo So ce fs Ca NO) Co al on cnar ssc te eal er pel ds al Sp ciate rssh eon gd sme mpant Scronmo asd wc on The ponte gare and serves red hy the gener tem cfr ‘melee, coca te See mea. get 80 Cg ne Aa forte cc ean ease The genera wo opengl er ins Hedrons wich case he byte cue. Thos peony, ‘erp, wes stg othe way =) Osiderdectass seh tbh don acon, Sonharen nd omeree hs) rarangenen ef Cen th cathe cage of C-0, C-N, CC bo of eer te ror dle nts Thy cana can te etn co ose banal hy can case te wats ches he nls scorn sh ‘ease dO, (Sree ESE —<$<$<$<~__—— sarees coccinea a fos ee at Laver meal tring with éve DNA bases destabilise Se otro te Pete open rar ica eee fee Sas am Ph ea ct se ee ence ay Sees ies an, eee nares ae Sree gatas eee ty eee ae ee na fee ae Teun lbs beso force inci neato a reenter eT nen ik’ noe, Now nat eh nt ds ‘init Du nem rimeain prt at pt polo hrc stitch Oh akc tn one ‘rte days and hen © can ncn and ows snes NO ea eS acetate reer Ree eae oe ene Soom te sent oles make tinal Bot bw meta real cd chet amo er sil rH, re i etl ee 9 wales tanta: a det me cups co Seon Ce mn ea ry ee Seem 235.1 Mh on et the pct cen AO Pa See 1481), “hs cogil radeon nay ve dif pili esl secon ear Inte on rater sie oD tale rane fa 2 a ‘Merrion of ona sm. on ooh “The pct tot tl le rea meoamey hae mnie 2.3.6 Matl ons in econ Transport Process The peite rtapsa eorng bs pore ke Bu potent ‘ee FS pris Fete" coal as ocomens Fe™ Re capt Te ‘edi Chaser ‘24 THE ROLE OF METAL IONS IN THE BASI OLOGICAL REACTIONS. ‘The ct impart tne eal recom a Satna, ton, loge ‘alo, lease and ome meee eer Proto Sc 8.5) ti rc, sla egy coed no chen ew betoclermagterrernsee ature let olen he hs johansson ones o ck agente fuason pny an impos co SAP ato corer of bach erry = [ATP alin phesphoroton proses hen ao ee ‘nt bsp 1 tapi nl ompite nf 960" oe ‘Beis te ton pr Eve prs 32 se pa ‘arm atom 30 fa 1 a pin ma nee atthe chal parma AB ZONA we compen Te 38 ante 204 Chri lees Rand ONAL 25:11) =F a 7a =m etme peimees [Ragtime | tied 6 seeren pees | (Talia Tefen senate) 2 ” + Yaesu “som bet | 20 1 trp tp pe sem Saint ‘nese ‘renee 04| 8 re) eer oben eau! how the sat tae eg hen ol mn aie st Th rnenasn ey gut vgn nd ede pp ‘a eee reece ymnery ol i a mach ah hcl Trentonian pra Rapala swe ay rly of he mica nt Fee pote Bung ot Rr compe me minor soe ba wan, = croissant ‘Sclner een Tor pow bsg of Rape tuple mah we Sere aebchevncsoaok emus cl gee ee nw geome iol aac, te Sgn of omer ne end wi 0 Prt of haphnerSgs :Cmdrtin ty mil ee eh er ‘Bosch bodkonan onic tps opted BNA (u) Damage to Watson- sn Sep! exe ny coh compre fon ae a en et Dlnmmilyse comin Conc win asthe a ecg Zhong en a eb nD 2 158 thauuren wan std se be seed bcos may ‘els fn ren tcsun, fe threo nt we aed, Now {She nba of Encoder he ben ahi te hc Blog a Datu selection of Zn in hi ncle aid ding preening erm redox sty whch could damage the DNA ein the ene re LT hecter maa re el te! Oe DRA Rae riche lel str ‘Seal 2 depend DNA and RNA pea ar nw eid eT cron en et ce eae La ‘Scarce nr yene eprnion a th lca en Mile ey dpe en Znceent ‘Stal The beh wet ard ad cans wea ut cape leno (San im ner pement mothers rie er Sn of 2 Tis are asa rs ‘ppun bctt ngrowth car Sane psf hopes beni den te (Siow cif 2 char srranton of 1, HO an pre anion Zod gute common UK ad ter ten a eto owing cae - {0 Gs of phosphate erence Zo echt 2oJPO, wich ener Za et ey Sata the ronal meet 9 Decreased organics i te apt a aces ‘Nonwal rgarc ching ae an se | RISES me for pn epee On he gare ct ‘herenadia 2-0 compas wth 1026 ahora nnn ah toa na cup rt ace cea Inwolve the eatavtic cles live Fe? /Fe™ or Cul /Cur, 2 en rvs oa oe {Bh comple wth contin mtd 6 merc fans [poe ober rcp on on ae oon eZ) of nae Fran ae ios Soe citer ca ter (2) oa cd ect: a be ayn at 2 no ci | fs amtarng eats of sa Thee wm oo Sng es {acter po DNA ot NA pls Tete tae con Sin nce svt (a nen sac any oe ae cn ae 2s esa eon tty roy Gane BNA at of Fo {iy 2 Sst crt one be certo err wh Ftc potely to pret Fe tnt Zn reassert fro he fot pe funnel nein Se Eel may dongle en sre 5 443 Binding Se of Zt i Protein = Cty od Srl Stes ney aie eon ae aa : aa peranretel apap ane fesse. uve Savas ares Rieti rane a Sa - ‘iste at nd nd ptt, ran ah Et i ets Pec ae, oe wat sere Somme ey me pete ee rn el a niet Sorte Cay owe t= pe ml el ae 0 ma 9255 [erect am bor ie ci let hn Be iy oe ti Peper chemistry. Crin ts higher oxtion = — oes pans nut roca acyroame — | Rate | zee amen meee 36 tee oct ae esate ap sae a, oP Mor sarsce rookie orate see esa tc tocar men ne ip ume ie lit leper Nop assy th etree hea Ufonmolidenum oactor Lr Felco pnt =e neoprene re ar one igen ten Sacer fennel ello he men cared nee 33 Mikel: Nut cece inert care oma ter bt tl oe (Seri ate ese Tener = a omer of Ca san et 100 cone ty the mono ee ‘ce frm tans D ch eon ee Scher eno plane es etcetera th i ol of in a CaP ce ys ean, are a on ‘ting eps! cong nn sr aco rope SNE" my con aa en ee uh ees et Tilia, ajpems gina neared be ee ei aa a gn ‘Bowne rary ctor teu an poor fa cot one abe rp msc PSST chic mentite wo ove amino sir 1G moo! tr ee esa Yerba oat. Bhskovesnc ns irephtin mace, Ca" tera wah parame (CE ora ding actson of ser pc 2.744 Colmedoln (Co lon Corin) Caksen ion (C2 ted Yo actate a ruber of ene Aine) Probst, dng an cae property For is purpose, We el nade 3 le ‘Set on oa Ca depandet teh ot es ‘Simul (CM) prover Mel We = 17 KDa i haa ge itpmte aod ghtamatel” The mole aw dumb ‘nected antes. Eh ou ema conta 0 Ca" \Grvlind i ooperatue menner uth higher Bring coor ‘nd wih relate lover fy. The calmed protein ‘formation with the tindiog and removing af Cat fon. The Cina ‘ntsc nth the ret ten or engme Ee oat the rotamer ene. tout the ‘ning, calmodulin nace to meas and fo atte te fre prs ad ene Ca cx" —= cao, — carat, Ee 6 pemeort Treen, moun nase, ich neat mosinactin ‘oll nati” a de yo C2 fauna ‘pre ome Ks, AP, and prot ok in penethrn nda we ety ol ct vetom pts Wek on shits he camo fon ‘ion ‘eit Ca Irflammotory can (Se 1215) an abo onsieing oct Se er “Tent ath tn Th ane psy (TFator Xe Por pcos ot ee Forge cesta te ae aren ew racers 4s Factor, oom " ourmaiote) Prsamwon en) FCO te* FR cr menses r i Ft racy * pose, cah roe or x ctr Facore, oem, oe re pa Cnaar sche. ot pein od aig pe nin pa) Fe 3 ween nen ag on es a iti oo ee SEsinot ace e Fancy anew aon Sig Ti Seer tl et ese na Spa sieemtin enor cesta are i oer eon eer Poneto erect as Se meer ee ee hy Sane lt mn are te soe on a Ores agien eee Nee iene oe qaoniame Cane pe re Aeooo oer ae Posh ilar Tar So or ene aces oe ‘Appr i ms of mle elaine, he mle caton My shal ted mot ‘roy snp tt te tl eg er ch lily rd he eet lo ‘Sem rte chan ae alroin a ua oheth t atn ath he ao ps {2 rte ee rors he clmodin, Trp C, pram, ce Cae ets ‘lacy ecogne Ca enn te peer ty gh cota ‘pane protein works du othe fscared Ca pn raion ‘Slop the higher coriatin ‘umber ha Ma eng ret number grote ha seo th tino. Forearm Ce ‘tog than Mw the Casepe poten albumin lel EF Pod fer Satiey tt omreeetnn itehy, Cais slctey ed arg" be rte Tabte 3.82 Sety proc a3 p= 5.) seme alee i Soo fan wom, 9, Manan a sche vob ee fom ee concn 100 0 oe ep eed wih fr energy chat (apt ode cc nt moa sy pcin r r ireper whee forse conse ACh epost Thos pons Tope teresa fred rd Wen gon poe whe tho Perea actrees eee as Ca rr an care nh lacie ce the mere a pct gt tee | aT el mentrre he st 70 Ao campo ten srt ‘ois ie Pa 1311” Caen rmot Shi lr aoa te re Chey fe ly deg corer wc urt nde an ele ‘pe dela fe mee eh an te me ie nme chan hg nals ne are ‘exile chee! evel ay NAC at eh eo th ed tenmte, 12 Pcs Ma gt AT RO tet Ane ito Aaentero bunt, (aa sere tr ees cto pc, eon, ny tp ne shady he concenton re the sey ict ced OB Chr = Cua ct ey ‘iste te content Gi Donnan Equa Anan he eos, Co” aN aera erent bay ie ie sate wl Kw scene mea T a exer he Sree yp scar Fors pales onan aro B= SEorIe UAL, = 2 ML /migie 10, (enya = 100. The comers (eral dt of ew nt ear cia hao ot ri i oe xray fd N01), K° (005, Intacar 119091 KO) ‘Tag ompnton the eal dine af sot Te cen ‘marcy the aa lh ae CT HCO,” SOG" and PO To aah «ep Srcntatc gtr Na, KY Ma" od Can aed ey nie te Seto TP ————— “These ee ca com herbals Signi saeit versiesie to aa Dioeont Beran KGa Ne 9 Ut a eigen eran Coa ‘he ced bney ofthe eer oman oH Go eb comp sien he cexgzmie The Om ba omnia ators notated ‘Ste to cane ger we a he Gee ane won: ow wan eset mace fet Hf S18 ete AS hes bam more sae coop compu Toe tein open Ma ea ‘hme, CHOCH,CHL OCH. Darra semen, seinen oft atl en enn cmt te shed cn oe inc Cnltaon Teenie he cr SRS Seer! (aT, Tx emp ng at Wace te (ling seer erie tact te she ne macmost he ny HOSEN" uch tee a he outa tring le a= wit Beta ldtoorcon te compere’ by scared eto actr U aS= i) The Sk SPECI dr coin wake 85 nr pot Fors sae own ee erste eta trian 2 het ta which dries he ‘Sola nabs rit, the ue’ hs ef the coum ther Oo HD. Be ‘morn ror fo cham the cnfomaton ofthe mate da reorgmiation| ‘Sapcnt ard ecsy uae mel se the es port conaeatons SLES cnt han tt ozsoon th moe yo be owe com “Tonics be ong cf maces fe it cna ter coin oo serine tshirt compe th ba marc a. row dhe ‘Setpoint pont penta CH i Odmot!) | AS etal) =560 ~no | =m0 reed th sa to opti Meee ecom te 85300 ‘pt ,1,11 (10 p< p21 160 p< ep. 2,.2 (280 pn

    You might also like