Electron Transport and Oxidative Phosphorylation

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Figure 20.13 The structure of mitochondrial cytochrome c. The heme is shown at the center of the structure, covalently linked to the protein via its two sulfur atoms (yellow). A third sulfur from a methionine residue coordinates the iron. Garrett and Grisham, Biochemistry, Third Edition
Garrett and Grisham, Biochemistry, Third Edition Complex IV Transfers Electrons from Cytochrome c to Reduce Oxygen on the Matrix Side Cytochrome c Oxidase • Electrons from cyt c are used in a fourelectron reduction of O 2 to produce 2H 2 O • Oxygen is thus the terminal acceptor of electrons in the electron transport pathway - the end! • Cytochrome c oxidase utilizes 2 hemes (a and a 3 ) and 2 copper sites • Structure is now known - mostly! • Complex IV also transports H +
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: Figure 20.12 The Q cycle in mitocho
Page 25 and 26: Figure 20.16 Molecular graphic imag
Page 27 and 28: Figure 20.18 (a) The Cu A site of c
Page 29 and 30: Figure 20.20 A model for the mechan
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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