Electron Transport and oxidative phosphorylation (ATP Synthesis) Dr. Abir Alghanouchi Biochemistry department Sciences college

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1 Electron Transport and oxidative phosphorylation (ATP Synthesis) Dr. Abir Alghanouchi Biochemistry department Sciences college

2 All of the reactions involved in cellular respiration can be grouped into three main stages Glycolysis occurs in cytoplasm The Krebs cycle occurs in matrix of mitochondria Electron transport occurs across the mitochondrial membrane 2

3 Process in which ATP is formed as a result of transfer of electrons from NADH or FADH 2 by a series of electron carriers The electron transport chain generates no ATP directly. Rather, its function is to break the large free energy drop from food to oxygen into a series of smaller steps that release energy During respiration, most energy flows from glucose > NADH > electron transport chain > proton motive force > ATP. 3

4 Oxidative process Phosphorylation process inner membrane O 2 e - H 2 O H + ADP+ Pi H + ATP ATP Synthase outer membrane matrix intermembrane space Figure: Essential features of oxidative phosphorylation Redox reactions of respiratory chain use electrons to reduce oxygen to water Energy generated moves protons from matrix to intermembrane space Inward movement of protons recovers this energy to promote formation of ATP in the matrix. 4

5 Protein complex Electron carrier Inner mitochondrial membrane Electron flow Electron transport chain ATP synthase 5

6 ATP yield Only 4 of 38 ATP ultimately produced by respiration of glucose are derived from substrate level phosphorylation (2 from glycolysis and 2 from TCA) The vast majority of the ATP (90%) comes from the energy in the electrons carried by NADH and FADH 2 6

7 Cytosol High-energy electronscarried by NADH High-energy electrons carried mainly bynadh Mitochondrion Glycolysis 2 Glucose Pyruvic acid 2 Acetyl CoA Krebs Cycle Electron Transport Maximum per glucose: by direct synthesis by direct synthesis by ATP synthase A Road Map for Cellular Respiration 7

8 Chemical reactions that transfer electrons from one substance to another are called oxidation reduction reactions REDOX short for oxidation reduction reactions 8

9 REDOX FACTS A:H A Reductant Oxidant + e B B:H Oxidant + e Reductant (acceptor) (donor) Both oxidation and reduction must occur simultaneously The reductant of one pair donates electrons and the oxidant of the other pair accepts the electrons Red1 (AH) + Ox2 (B) Ox1(A) + Red2(BH) 9

10 Electrons can move through a chain of donors and acceptors In the electron transport chain, electrons flow down a gradient Electrons move from a carrier with low reduction potential (high tendency to donate electrons) toward carriers with higher reduction potential (high tendency to accept electrons) 10

11 Potential (E O ): measure of the tendency of oxidant to gain electrons, to become reduced, a potential energy. E O : Standard reduction potential difference between two half reactions 11

12 Succinate E o = 0.03V E o = 0.07V II NADH I Coenzyme Q E o = -0.32V E o = 0.10V E o = 0.42V III E o = 0.19V electron flow Cytochrome C E o = 0.29V E o = 0.53V IV ½O 2 E o = 0.82V The components of the RC are arranged in order of increasing redox potential The Eo values are the potential differences across the four complexes ( that span the mitochondrial inner membrane) 12

13 Succinate E o = 0.03V E o = 0.07V II NADH I Coenzyme Q E o = -0.32V E o = 0.10V E o = 0.42V III E o = 0.19V Cytochrome C E o = 0.29V E o = 0.53V IV ½O 2 E o = 0.82V electron flow The overall voltage drop from NADH E 0 = ( 0.32 V) to O E 0 = V is Eº = 1.14 V 13

14 RC exists as four large, multisubunit protein complexes The respiratory electron transport chain complex I is a NADHubiquinone reductase complex II is succinate dehydrogenase complex III is the ubiquinone cytochrome c reductase complex IV is cytochrome oxidase 14

15 Figure: Complex I of the respiratory chain that links NADH and coenzyme Q. NADH Dehydrogenase (NADH ubiquinone reductase) accepts 2e from NADH and transfers them to ubiquinone (coenzyme Q), an electron carrier Uses two bound cofactors to accomplish this: FMN (Flavin mononucleotide) and 6 iron sulfur (Fe S) protein 15

16 Complex II: Succinate-CoQ reductase Prosthetic groups: FAD; Fe-S Succinate FAD SDH Fumarate FADH 2 CoQ SDH is succinate dehydrogenase an enzyme of the citric acid cycle (associated with membrane) 2 e transferred from succinate to CoQ 1 mole FADH 2 produced 16

17 Electrons from complex I or II Complex III: cytochrome reductase Prosthetic groups: heme b; heme c 1 ; Fe-S CoQ cyt b/cyt c 1 cyt c Figure: Complex III of the respiratory chain linking CoQ and cytochrome C. Is composed of cytochome b, cytochrome C 1 and iron sulphur proteins Accepts e from coenzyme Q and transfers e to cytochrome c coupled with the transfer of protons from the matrix to the intermembrane space 17

18 Figure: Complex IV cytochrome oxidase reducing oxygen to water Contains cytochromes a/a3 and 2 Cu ions involved in e transfers Cytochrome oxidase passes electrons from cytochrome c through a series of heme groups and Cu ions to O 2, reducing it to H 2 O (end product) 18

19 Coenzymes and cytochromes in the complexes act as e donors & acceptors 19

20 Flavin MonoNucleotide (FMN), in Complex I, functions like FAD (which is an electron acceptor that helps electron transfer during Krebs Cycle and Electron Transport Chain in cellular respiration). iron sulfur (Fe S proteins): Fe S centers transfer e in Complexes I, II and III Coenzyme Q (ubiquinone), lipid soluble, floats in the membrane and doesn t require protein Cytochromes (b, c 1, c, a, a 3 ; contain heme): transfer e in Complexes III and IV, Cytc is the only soluble cytochrome NAD+, FMN, CQ are carriers of e and hydrogen while cytochromes are carriers of electrons only. 20

21 ATP synthase (complex V), present in the inner mitochondrial membrane, actually makes ATP from ADP and P i. ATP used the energy of an existing proton gradient to power ATP synthesis. This proton gradient develops between the intermembrane space and the matrix. This concentration of H + is the proton motive force. 21

22 The ATP synthase molecules are the only place that will allow H + to diffuse back to the matrix This flow of H + is used by the enzyme to generate ATP a process called chemiosmosis. Chemiosmosis: (osmos = push) is the oxidative phosphorylation that results in ATP production in the inner membrane of mitochondria. 22

23 Properties of ATP Synthase Multisubunit transmembrane protein Molecular mass = ~450 kda Functional units F 0 : water insoluble transmembrane protein (up to 8 different subunits) F 1 : water soluble peripheral membrane protein (5 subunits),contains the catalytic site for ATP synthesis Flow of 3 protons through ATP synthase leads to phosphorylation of 1 ADP 23

24 Cytosolic NADH (glycolysis) must enter the mitochondria to fuel oxidative phosphorylation but NADH and NAD + cannot diffuse across the inner mitochondrial membrane Two shuttle systems for reducing equivalents: 1. Glycerol phosphate shuttle: insect flight muscles 2. Malate Malate aspartate shuttle: predominant in liver and other mammalian tissues 24

25 25

26 In muscle and brain Each NADH converted to FADH 2 inside mitochondrion FADH 2 enters later in the electron transport chain Produces 2 ATP 26

27 27

28 In liver and heart NADH oxidized while reducing oxaloacetate to malate Malate dehydrogenase Malate crosses membrane 28

29 Malate reoxidized to oxaloacetate Malate dehydrogenase NAD + reduced to NADH NADH via electron transport yields 3 ATP 29

30 Respiratory inhibitors These compounds prevent the passage of e by binding a component of the ETC blocking the oxidation/reduction reaction 30

31 31

32 Complex designation I NADH-Q reductase II Succinate- Q reductase III - Cytochrome reductase IV - Cytochrome C oxidase Functional groups Function FMN (flavin oxidizes NADH to NAD + ; mononucleotide); transfers electrons to Fe S coenzyme Q FAD; Fe S heme b; heme c 1 ; Fe S heme a a 3 ; Cu oxidizes succinate to fumarate with reduction of FAD to FADH 2 ; electron transfer to CoQ transfers electrons between coenzyme Q and cytochrome C (C becomes reduced) oxidizes cytochrome C; reduces ½O 2 to H 2 O Inhibitors Rotenone Antimycin A Carbon monoxide Cyanide

33 Lippincots Illustrated Reviews Biochemistry Lechingers Principles of Biochemistry 4th edition. D. L. Nelson and M.M. Cox, Worth Publishers. Harpers illustrated biochemistry 25 th edition. Robert K. Murray; Darly K. Granner: Victor W Rodwell

34 34

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