Figure 14.1 Energy relationship between energy production (catabolism) and energy utilization (anabolism). Textbook of Biochemistry with Clinical Correlations,

Figure Energy relationship between energy production (catabolism) and energy utilization (anabolism). Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.2 Structure of ATP and ADP complexed with Mg2+
Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.3 Oxidation states of typical carbon atoms in carbohydrates and lipids.

Figure 14.4 Transfer of reducing equivalents during catabolism and anabolism using NADPH and NADH.

Figure 14. 5 (a) Resonance forms of phosphate
Figure (a) Resonance forms of phosphate. (b) Structure of pyrophosphate. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.6 Hydrolysis of phosphoenolypyruvate indicating the free energy released.

Figure 14.7 Examples of reactions involved in transfer of “high-energy” phosphate.

Figure 14.8 Nucleoside diphosphate kinase and nucleoside monophosphate kinase reactions.

Figure 14.9 Adenylate kinase (myokinase) reaction.

Figure 14.10 General precursors of acetyl CoA.

Figure 14.11 Structure of acetyl CoA.

Figure 14.12 Metabolic fates of pyruvate.

Figure 14.13 Pyruvate dehydrogenase complex from E. coli.

Figure 14.14 Mechanism of the pyruvate dehydrogenase multienzyme complex.

Figure 14.15 Regulation of the pyruvate dehydrogenase multienzyme complex.

Figure 14.16 Sources and fates of acetylCoA.

Figure General description of oxidation of foodstuffs to provide energy for ATP synthesis within mitochondria. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.18 The tricarboxylic acid cycle.

Figure Structures of succinate, a TCA cycle intermediate; malonate, an inhibitor of succinate dehydrogenase, and the cycle; and maleate, a compound not involved in the cycle. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure The TCA cycle is a source of precursors for amino acid, fatty acid, and glucose synthesis. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.21 Sources and fates of succinyl CoA.

Figure 14.22 Anaplerotic reactions replenish intermediates of the TCA cycles.

Figure 14.23 Pyruvate carboxylase reaction.

Figure 14.24 Examples of regulatory interactions in the TCA cycle.

Figure 14.25 Mitochondrial structure.
(a) Electron micrograph of mitochondria in hepatocytes from rat liver (39,600). (b) Electron micrograph of mitochondria in muscle fibers from rabbit heart (39,600). Courtesy of Dr. W. B. Winborn, Department of Anatomy, University of Texas Health Science Center at San Antonio, and the Electron Microscopy Laboratory, Department of Pathology, University of Texas Health Science Center at San Antonio. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.26 Diagram of submitochondrial compartments.

Figure Overview of the complexes and pathways of electron transfer in mitochondrial electron transport chain. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure Oxidation-reduction potentials of the mitochondrial electron transport chain carriers listed from the most negative (NAD+/NADH) to the most positive (O2/H20). Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.29 Model of the crystal structure of the hydrophilic domain of complex I.
Reprinted with permission from Sazanov, L. A. Biochemistry 46:2276, Copyright (1977)by American Chemical Society. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.30 Structures of iron-sulfur centers.

Figure 14.31 Oxidation-reduction of ubiquinone (coenzyme Q).

Figure Reduction of ubiquinone (UQ) in the mitochondrial inner membrane by the flavoproteins NADH, succinate, glycerol 3-phosphate, and fatty acyl CoA dehydrogenase. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.33 Model of the crystal structure of the dimetric cytochrome bc1 complex.
Reproduced with permission from Kim H., Xia, D., Yu, C.-A., Xia, J.-Z., Kachurin, A. M., Zhang, L., Yu. L., and Deisenhofer, J. Proc. Natl. Acad. Sci., USA 95:8026, Copyright 1998, National Academy of Sciences, USA. Figure generously supplied by Dr. J. Deisenhofer. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.35 Structures of heme a1 heme b1 and heme c.

Figure 14.36 Six coordination positions of cytochrome c.

Figure Model of crystal structure of cytochrome c oxidase from bacterium Paracoccus denitrificans. Reproduced with permission from Iwata, S., Ostermeier, C., Ludwig, B., Michel, H., et al. Nature 376:660, Copyright © (1995), Macmillan Magazines Limited. Figure generously supplied by Professor S. Iwata. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure Binuclear center of cytochrome c oxidase indicating heme a3 and CuB. L is an unknown but proposed ligand. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.39 Pathways of electron and proton transfer through cytochrome c oxidase.

Figure Overview of mitochondrial electron transport chain indicating locations of complexes I-IV, ubiquinone (CoQ) and cytochrome c in the inner membrane, pathways of electron transfer, and sites of proton pumping. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure The electrochemical gradient consists of a gradient of charges ( ∆ ) and proton concentration (∆pH) across inner mitochondrial membrane. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure Demonstration of coupling of electron transport to oxidative phosphorylation in a suspension of liver mitochondria. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.43 Inhibition and uncoupling of oxidative phosphorylation in liver mitochondria.

Figure Action of the uncoupler, 2,4-dinitrophenol, a proton ionophore which equilibrates pH across the inner mitochondrial membrane. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.45 Electron micrograph of mitochondrial F1.
Generously supplied by Dr. D. F. Parsons. From Parsons, D. F. Science 140:985, Reprinted with permission from AAAS. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.46 Model for mitochondrial F1F0-ATP synthase, a rotating molecular motor.

Figure 14.47 The binding change model for ATP synthesis by ATP synthase.

Figure 14.48 Mitochondrial ATP synthase complex.
Reproduced with permission from Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. Nature 370:621, Copyright © (1994 Macmillan Magazines Limited). Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.49 Mitochondrial metabolite transporters.

Figure 14.50 The adenine nucleotide translocase and phosphate transporter.

Figure 14.51 Transport shuttles for reducing equivalents.

Figure Export of citrate generated in mitochondria to cytosol where it serves as a source of acetyl CoA for biosynthesis of fatty acids or sterols. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.53 Mitochondrial calcium carrier.

Figure 14.54 Activation of UCP-1 by cold adaptation.

Figure 14.55 Map of genes on mitochondrial DNA.

Figure One electron steps in reduction of oxygen leading to formation of reactive oxygen species superoxide, hydrogen peroxide, and hydroxyl radical. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.57 The Fenton and Haber-Weiss reactions for formation of toxic hydroxyl radical.

Figure 14.58 Generation of superoxide anions by mitochondrial electron transfer chain.

Figure 14.59 Respiratory burst in phagocytes.

Figure Superoxide dismutase and catalase protect cells by removing superoxide and hydrogen peroxide. Textbook of Biochemistry with Clinical Correlations, 7e edited by Thomas M. Devlin © 2011 John Wiley & Sons, Inc.

Figure 14.61 Glutathione peroxidase removes hydrogen peroxide as well as lipid peroxides.

Figure 14.1 Energy relationship between energy production (catabolism) and energy utilization (anabolism). Textbook of Biochemistry with Clinical Correlations,

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Figure 14.1 Energy relationship between energy production (catabolism) and energy utilization (anabolism). Textbook of Biochemistry with Clinical Correlations,

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