Bioinorganic Chemistry

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1 Bioinorganic Chemistry Study of metal species in biological systems metal ion transport and storage, Metallohydrolase enzymes, metal-containing electron transfer proteins, oxygen transport and activation proteins, bioorganometallic systems such as hydrogenases and alkyltransferases, enzymes involved in nitrogen metabolism pathways.

2 Biological functions of selected metal ions Metal a, K Mg, Zn Ca V, Mo Mn Fe, Cu i Function Charge carrier, osmotic balance Structural, hydrolase, isomerase Structural, charge carrier itrogen fixation, oxidase Photosynthesis, structural, oxidase Dioxygen transport and storage, electron transfer, oxidase hydrogenase, hydrolase

3 a Mg K Ca Sc Ti V Cr Mn Fe Co i Cu Zn Y Zr b Mo Tc Ru Rh Pd Ag Cd La Hf Ta W Re s Ir Pt Au Hg aturally occurring in biology Used as probes

4 Chemical elements essential to life forms can be divided into the following (i) Bulk elements: C, H,,, P, S (ii) Macrominerals and ions: a, K, Mg, Ca, Cl, P 4 3-, S 4 2- (iii) Trace elements: Fe, Zn, Cu (iv) Ultratrace elements comprises of (a) non-metals: F, I, Se, Si, As, B (b) metals: Mn, Mo, Co, Cr, V, i, Cd, Sn, Pb, Li

5 Essentiality of elements is defined by (1) A physiological deficiency appears when the element is removed from the diet (2) The deficiency is relieved by the addition of that element to the diet (3) A specific biological function is associated with the element

6 Every essential element follows a dose-response curve

7 At lowest dosages organism does not survive In deficiency regions, the organism exists with less than optimal functions After optimal dosage (plateau region), higher dosage cause toxic effects in the organism eventually leading to lethality

8 Active Site and Enzyme Substrate Complex The active site of an enzyme is the region that binds the substrate and contributes the amino acid residues that directly participates in the making and breaking of chemical bonds Generalizations 1) Enzymes are usually very large compared to the substrate nly a small portion is involved in ES complex Rest portion is involved in control and maintaining of structure

9 2) The substrate is bound by relatively weak forces ΔG E-S complex = (12 to 36) KJ mol -1 (strength of a covalent bond is upto ~ 450 KJ mol -1 ) 3) Active sites are designed to exclude H 2 Surrounded with non-polar amino acids to create a hydrophobic environment Essential for substrate binding and product formation (Catalysis)

10 Specificity Active site provides specificity for its particular substrate Substrate has a matching shape to fit into the active site (Lock and Key mechanism) Formation of Enzyme-Substrate Complex is thus crucial to the product formation

11 Evidence for Enzyme-Substrate Complex (1) At constant [E], increasing the [S] will increase the reaction rate until a maximum velocity is reached, (2) Isolation of E-S complex (3) X-ray diffraction studies of E-S complex (4) Spectroscopic studies of E-S complex

12 Active sites of Enzymes His() Zn Glu() His() H 2 peptide hydrolysis (removes terminal amino acids f rom proteins) Carboxy peptidase His() His () Zn H 2 H 2 + C H 2 C 3 H + + HC 3- His() Carboxy anhydrase Cys(S) AD + ADH Cys(S) His() Zn H 2 CH 3 CH 2 H CH 3 CH Liver Alcohol dehydrogenase

13 Hemoglobin Active-Sites of Enzymes C 2 - C 2 - Fe II C 2-2 Fe II C 2 - Hemocyanin Hemerythyrin H H H H H H H 2 Cu I CuI Cu II H Fe II H Fe II H H H 2 H H H H H Fe II H H Cu II Fe III H h H H H

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15 Porphyrins Porphyrins are tetrapyrrole macrocycles with conjugated double bonds and various groups attached to the perimeter R R R H H R R R R R variation of substituents facilitates the tuning of electron-donating and electron-withdrawing ability of the ligand

16 The porphyrins can accept two hydrogen ions to form+2 diacids or donate two protons to form -2 dianions Porphyrins are found in many metalloenzyme Enzyme Function Fe-porphyrin Cytochrome electron transfer Fe-porphyrin Mg-porphyrin Hemoglobin Myoglobin Chlorophyll dioxygen carrier photosynthesis

17 Cytochromes Cytochromes are electron transfer proteins There are three types of cytochromes depending upon the porphyrin types cytochrome a, cytochrome b, cytochrome c H H s-cys protein s-cys protein Fe Fe Fe H H a H H b H H c H

18 The prosthetic group in all cytochromes comprises of four heme units They have a molecular weight of about 12,400 Active site differences between Hemoglobin and Cytochrome S (cys) Fe Fe (His) Hemoglobin (His) Cytochromes

19 Depending upon the ligand, the redox potential of a given cytochrome can be tailored to meet specific need in electron transfer schemes (photosynthetic versus respiration) The potentials are such that the electron flow is from b c a 2 Cytochrome a is capable of binding 2 and reducing them Cytochrome a is responsible for severe toxicity of C - C - binds to the 6 th site and stabilize Fe III to such an extent that it cannot participate in electron transfer schuttle

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25 Hemoglobin Fe II Fe II (His) High Spin paramagnetic t 2 g 4 e g 2 Deoxyhemoglobin (His) Low Spin diamagnetic t 2 g 6 e g 0 xyhemoglobin Deoxyhemoglobin is the form of hemoglobin without the bound oxygen. The oxyhemoglobin has significantly lower absorption (660 nm) than deoxyhemoglobin (940 nm). This difference is used for measurement of the amount of oxygen in patient's blood by pulse oximeter.

26 The size of Fe 2+ increase by 28% on going from Low spin (oxyhemoglobin) (0.61 Å) to High spin (Deoxyhemoglobin) (0.78 Å) The Fe 2+ in deoxyhemoglobin is too large to fit in the ring and is situated ( )A o above the ring Thus, presence of 2 changes the electronic arrangement of Fe 2+ and distorts the shape of the complex The globular protein prevents the irreversible oxidation of Fe(II) to Fe(III)

27 When 2 binds to one sub-unit Cooperativity Fe 2+ contracts, moves into plane of porphyrin ring triggers conformational changes in the globin chain moves the histidine attached to it translated through H-bond network Enhances the ability of other three units to bind 2 This phenomenon is called cooperative effect In a similar way when the blood reaches the muscle, only one 2 is released, the others are released even more easily due to the cooperative effect in reverse

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29 picket fence porphyrin

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