Electron Transport and Oxidative Phosphorylation

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Figure 20.19 The binuclear center of cytochrome oxidase. A ligand, L (probably a cysteine S), is shown bridging the Cu B and Fe of heme a 3 metal sites. Garrett and Grisham, Biochemistry, Third Edition
Figure 20.20 A model for the mechanism of O 2 reduction by cytochrome oxidase. (Adapted from Nicholls, D. G., and Ferguson, S. J., 1992. Bioenergetics 2. London: Academic Press; and Babcock, G. T., and Wikström, M., 1992. Nature 356:301-309.) Garrett and Grisham, Biochemistry, Third Edition
Page 1 and 2: Chapter 20 Electron Transport and O
Page 3 and 4: Garrett and Grisham, Biochemistry,
Page 5 and 6: Figure 20.1 (a) A drawing of a mito
Page 7 and 8: Figure 20.2 Experimental apparatus
Page 9 and 10: Figure 20.3 E o΄ and E values for
Page 11 and 12: Figure 20.5 (a) The three oxidation
Page 13 and 14: Figure 20.6 Proposed structure and
Page 15 and 16: Figure 20.7 The fatty acyl-CoA dehy
Page 19 and 20: Figure 20.10 The structures of iron
Page 21 and 22: Figure 20.12 The Q cycle in mitocho
Page 25 and 26: Figure 20.16 Molecular graphic imag
Page 27: Figure 20.18 (a) The Cu A site of c
Page 31 and 32: Figure 20.21 A model for the electr
Page 33 and 34: Figure 20.24 Molecular graphic imag
Page 35 and 36: Figure 20.26 ATP production in the
Page 37 and 38: Figure 20.28 The reconstituted vesi
Page 39 and 40: Figure 20.29 The structures of seve
Page 45 and 46: 20.6 - What Is the P/O Ratio for Mi
Page 47 and 48: Figure 20.33 The glycerophosphate s
Page 49 and 50: The Net Yield of ATP from Glucose O

Electron Transport and Oxidative Phosphorylation

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