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compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Focusing on the mechanism linking complex I and ATP synthase depicted in figure 3 in the article, compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

matrix side or n side NADH+H+ NAD+ complex I VUU ooo putative proton current by Brownian motion ADP + Pi a subunit DG F1 ATP synthase ОН ОН ОН ОН <d HOFO ATP synthase HO OH OH putative proton tunnelling through a subunit ATP U ОНОН ОН ОН ОН beepooooooo glutamic 58 of c subunit periplsmatic side or p side Figure 3. A possible H* circuit inside respiring membrane. The phosphate groups of phospholipids on both sides of the membrane are shown by brown ellipsoids. The image proposes that the H+ (red dotted line) are transferred to the Glu 58 (E58) at the centre of subunit c through subunit a of ATP synthase by proton tunnelling. H+ would flow from the periplasmic side, always bound to phospholipid heads. This can be arranged in each layer of the membrane.
Transcribed Image Text:matrix side or n side NADH+H+ NAD+ complex I VUU ooo putative proton current by Brownian motion ADP + Pi a subunit DG F1 ATP synthase ОН ОН ОН ОН <d HOFO ATP synthase HO OH OH putative proton tunnelling through a subunit ATP U ОНОН ОН ОН ОН beepooooooo glutamic 58 of c subunit periplsmatic side or p side Figure 3. A possible H* circuit inside respiring membrane. The phosphate groups of phospholipids on both sides of the membrane are shown by brown ellipsoids. The image proposes that the H+ (red dotted line) are transferred to the Glu 58 (E58) at the centre of subunit c through subunit a of ATP synthase by proton tunnelling. H+ would flow from the periplasmic side, always bound to phospholipid heads. This can be arranged in each layer of the membrane.
+ b. + Inner membrane + + 4 H + + 4 H+ 2 e NAD+ Inner membrane + + + + Dihydroxyacetone phosphate Glycerol-3-P dehydrogenase Succinate dehydrogenase + 2 e NADH + H+ -2 H+ FADH, Citrate cycle + Fumarate Succinate QH₂ NADH-ubiquinone oxidoreductase FADH₂ Glycerol-3-P 2 e + 2 e + FADH₂ 2 H Acetyl-CoA + QH₂ Fatty acids 2 H + 2 e 4 H Ubiquinone-cytochrome c oxidoreductase 2 H 2 x 1 e 4 H ETF-Q oxidoreductase Cyt c 2 x 1e Cyt c + + + Intermembrane space 2 x 1 e 2 e 2 H+ + O₂ H₂O IV 2 H+ Cytochrome c oxidase Mitochondrial matrix Intermembrane space 2x1 e IV 2 e 2 H+ 2 H+ O₂ H₂O matrix 2 H 2H+ Mitochondrial + Figure 11.8 Electron pairs (2 e) from NADH and FADH₂ flow through the electron transport system. a. Electrons from NADH enter the electron transport syster at complex I, then flow to coenzyme Q, complex III, and complex IV. A total of 10 H* are concomitantly translocated. b. Electron pairs are derived from FADH₂ oxidation at complex II (succinate dehydrogenase), from ETF-Q oxidoreductase of the fatty acid oxidation pathway, or from mitochondrial glycerol-3-phosphate dehydrogenase, which is part of the glycerol-3-phosphat shuttle. A total of 6 H* are concomitantly translocated when electrons are derived from FADH₂.
Transcribed Image Text:+ b. + Inner membrane + + 4 H + + 4 H+ 2 e NAD+ Inner membrane + + + + Dihydroxyacetone phosphate Glycerol-3-P dehydrogenase Succinate dehydrogenase + 2 e NADH + H+ -2 H+ FADH, Citrate cycle + Fumarate Succinate QH₂ NADH-ubiquinone oxidoreductase FADH₂ Glycerol-3-P 2 e + 2 e + FADH₂ 2 H Acetyl-CoA + QH₂ Fatty acids 2 H + 2 e 4 H Ubiquinone-cytochrome c oxidoreductase 2 H 2 x 1 e 4 H ETF-Q oxidoreductase Cyt c 2 x 1e Cyt c + + + Intermembrane space 2 x 1 e 2 e 2 H+ + O₂ H₂O IV 2 H+ Cytochrome c oxidase Mitochondrial matrix Intermembrane space 2x1 e IV 2 e 2 H+ 2 H+ O₂ H₂O matrix 2 H 2H+ Mitochondrial + Figure 11.8 Electron pairs (2 e) from NADH and FADH₂ flow through the electron transport system. a. Electrons from NADH enter the electron transport syster at complex I, then flow to coenzyme Q, complex III, and complex IV. A total of 10 H* are concomitantly translocated. b. Electron pairs are derived from FADH₂ oxidation at complex II (succinate dehydrogenase), from ETF-Q oxidoreductase of the fatty acid oxidation pathway, or from mitochondrial glycerol-3-phosphate dehydrogenase, which is part of the glycerol-3-phosphat shuttle. A total of 6 H* are concomitantly translocated when electrons are derived from FADH₂.
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