Bioenergetics
Nicholls, David G.; Ferguson, Stuart J.; Ferguson, Stuart
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Table of contents
- Cover
- CONTENTSv
- Prefaceix
- Note to the readerxiii
- Glossaryxv
- CHAPTER 1. CHEMIOSMOTIC ENERGY TRANSDUCTION3
- 1.1 Introduction3
- 1.2 The chemiosmotic theory: fundamentals3
- 1.3 The basic morphology of energy-transducing membranes7
- 1.4 Overview14
- CHAPTER 2. ION TRANSPORT ACROSS ENERGY-CONSERVING MEMBRANES17
- 2.1 Introduction17
- 2.2 The classification of ion transport17
- 2.3 Bilayer-mediated transport21
- 2.4 Protein-catalysed transport25
- 2.5 Swelling and the co-ordinate movement of ions across membranes26
- CHAPTER 3. QUANTITATIVE BIOENERGETICS: THE MEASUREMENT OF DRIVING FORCES31
- 3.1 Introduction31
- 3.2 Gibbs energy and displacement from equilibrium33
- 3.3 Oxidation–reduction (redox) potentials40
- 3.4 Ion electrochemical potential differences46
- 3.5 Photons47
- 3.6 Bioenergetic interconversions and thermodynamic constraints on their stoichiometries48
- 3.7 The equilibrium distributions of ions, weak acids and weak bases50
- 3.8 Membrane potentials, diffusion potentials, Donnan potentials and surface potentials52
- CHAPTER 4. THE CHEMIOSMOTIC PROTON CIRCUIT57
- 4.1 Introduction57
- 4.2 The measurement of protonmotive force59
- 4.3 The stoichiometry of proton extrusion by the respiratory chain66
- 4.4 The stoichiometry of proton uptake by the ATP synthase68
- 4.5 Proton current and respiratory control69
- 4.6 Proton conductance73
- 4.7 Mitochondria1 respiration rate and metabolic control analysis77
- 4.8 Overall parameters of energy transduction81
- 4.9 Reversed electron transfer and the proton circuit driven by ATP hydrolysis83
- 4.10 ATP synthesis driven by an artificial protonmotive force85
- 4.11 Kinetic competence of Δp in the proton circuit86
- 4.12 Light-dependent ATP synthesis by bovine heart ATP synthase87
- CHAPTER 5. RESPIRATORY CHAINS89
- 5.1 Introduction89
- 5.2 Components of the mitochondria1 respiratory chain89
- 5.3 The sequence of redox carriers in the respiratory chain95
- 5.4 The mechanism of electron transfer99
- 5.5 Proton translocation by the respiratory chain: 'loops', ' conformational pumps' or both?105
- 5.6 Complex I (NADH–UQ oxidoreductase)107
- 5.7 Delivering electrons to ubiquinone without proton translocation111
- 5.8 Ubiquinone and complex III (bc1 or UQ–CYT c oxidoreductase)114
- 5.9 Cytochrome c and complex IV (cytochrome c oxidase; ferrocytochrome c: O2 oxidoreductase)119
- 5.10 Overall proton and charge movements catalysed by the respiratory chain: correlation with the P/126
- 5.11 Superoxide production by complexes I and III127
- 5.12 Oxidative stress129
- 5.13 The nicotinamide nucleotide transhydrogenase130
- 5.14 Electron transport in mitochondria of non-mammalian cells131
- 5.15 Bacterial respiratory chains134
- CHAPTER 6. PHOTOSYNTHETIC GENERATORS OF PROTONMOTIVE FORCE157
- 6.1 Introduction157
- 6.2 The light reaction of photosynthesis in Rhodobacter sphaeroides and related organisms159
- 6.3 The generation by illumination or respiration of Δp in photosynthetic bacteria168
- 6.4 The electron-transfer and light-capture pathway in green plants and algae171
- 6.5 Bacteriorhodopsin and halorhodopsin186
- CHAPTER 7. THE ATP SYNTHASE195
- 7.1 Introduction195
- 7.2 F1 and F0195
- 7.3 The subunits of the F1.F0-ATPase198
- 7.4 The structure of F1.F0199
- 7.5 Enzymology of ATP synthase204
- 7.6 Relating the structure to function for ATP synthase210
- 7.7 Non-thermodynamic regulation of the ATP synthase216
- 7.8 Proton translocation by other ATPases and pyrophosphatases216
- CHAPTER 8. METABOLITE AND ION TRANSPORT219
- 8.1 Introduction219
- 8.2 Mitochondrial cation transporters220
- 8.3 Mitochondrial metabolite transporters225
- 8.4 The transfer of electrons from cytoplasmic NADH to the respiratory chain229
- 8.5 The phosphate and adenine nucleotide transporters230
- 8.6 The uncoupling protein family232
- 8.7 Bacterial transport234
- 8.8 Transport (movement) of bacterial cells246
- 8.9 Transport of macromolecules across bacterial membranes247
- CHAPTER 9. MITOCHONDRIA IN THE CELL249
- 9.1 Introduction249
- 9.2 Monitoring ΔΨm and ATP synthesis in intact cells251
- 9.3 Mitochondria and cellular Ca2+ homeostasis255
- 9.4 Mitochondria and programmed cell death258
- 9.5 Mitochondria and necrotic cell death261
- 9.6 The mitochondrial genome263
- 9.7 Import and assembly of mitochondrial proteins264
- 9.8 Mitochondrial genetic diseases266
- 9.9 Mitochondrial involvement in neurodegenerative diseases268
- References271
- Appendix. Protein structures283
- Index287
- Color Plate SectionPlate1
Book details
- Vendor Elsevier S & T
- SKU 9780125181211
- ISBN-13 9780080527932
- Author Nicholls, David G.; Ferguson, Stuart J.; Ferguson, Stuart
- Edition 3rd
- Category Science
- Subject Biotechnology
Do you have questions about this book?
This new edition of Bioenergetics presents a clear and up-to-date explanation of the chemiosmotic theory and covers mitochondria, bacteria, and chloroplasts. It takes account of the many newly determined structures, such as ATP synthase and the two photosystems of photosynthesis, that provide molecular insight into chemiosmotic energy transduction. This edition includes additional color figures of protein structures and many newly drawn illustrations designed to enable the reader to grasp the fundamental insights that are derived from knowing the structure. Every chapter has been extensively revised and updated and a new chapter on the study of the bioenergetics of mitochondria in the intact cell is included to satisfy the enormous interest in this topic. Written for students and researchers alike, this book is the most current text on the chemiosmotic theory and membrane bioenergetics available.
Key Features
* Chapter on the study of bioenergetics of mitochondria in the intact cell
* Appendix listing protein structure resources
* Additional colour plates of protein structures
* Many newly drawn illustrations
* Website
Key Features
* Chapter on the study of bioenergetics of mitochondria in the intact cell
* Appendix listing protein structure resources
* Additional colour plates of protein structures
* Many newly drawn illustrations
* Website
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