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E-Book, Englisch, 314 Seiten, Web PDF

Rao Sanadi Current Topics in Bioenergetics

Volume 10
1. Auflage 2014
ISBN: 978-1-4832-1694-2
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

Volume 10

E-Book, Englisch, 314 Seiten, Web PDF

ISBN: 978-1-4832-1694-2
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark



Current Topics in Bioenergetics, Volume 10 provides information pertinent to the developments in the study of dynamic mechanisms in functioning muscle by following fluctuations in kinetic states. This book explores the method that permits analysis of cyclic rotational motions in cross-bridge formation and has considerable potential in other bioenergetics systems. Organized into six chapters, this volume begins with an overview of the structure and function of muscles. This text then examines the bioenergetic aspects of nitrogen fixation. Other chapters consider one aspect of the regulation of the in vivo activity of organelles, namely, the regulation of mitochondrial activities at the level of substrate. This book discusses as well the status of the controversial findings on the proton-oxygen ratios in mitochondria and the mechanism of H+ pumping in oxidative reactions. The final chapter deals with the usefulness of bacterial mutants in the study of cell metabolism. This book is a valuable resource for biologists and biochemists.

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1;Front Cover;1
2;Current Topics in
Bioenergetics;4
3;Copyright Page;5
4;Table of Contents;6
5;List of Contributors;10
6;Preface;12
7;Contents of Previous Volumes;14
8;Chapter 1. Application of Fluctuation Spectroscopy to Muscle Contractility;18
8.1;I. Introduction;18
8.2;II. Occupation Number Fluctuations;22
8.3;III. Quasi-Elastic Light Scattering;49
8.4;IV. Prospects for the Future;59
8.5;V. Concluding Remarks;61
8.6;Acknowledgments;62
8.7;References;63
9;Chapter 2. Respiration-Linked H+ Translocation in Mitochondria: Stoichiometry and Mechanism;68
9.1;I. Introduction and Scope;69
9.2;II. H+ Translocation: Principles and Definitions;71
9.3;III. Translocation of Protons and Electrical Charge: Experimental Standpoints;75
9.4;IV. Stoichiometries from Thermodynamic and Related Steady-State Data;91
9.5;V. Special Aspects of the 02-Pulse Technique;95
9.6;VI. Proton Translocation in Submitochondrial Particles;99
9.7;VII. Proton Translocation in Reconstituted Systems;100
9.8;VIII. Mechanistic Aspects of Proton Translocation in the Cytochrome Chain;102
9.9;IX. Epilogue;110
9.10;Acknowledgments;110
9.11;References;111
9.12;Note Added in Proof;117
10;Chapter 3. Uptake and Release of Bivalent
Cations in Mitochondria1;120
10.1;I. Introduction;121
10.2;II. Basic Concepts of Ion Transport across Membranes;123
10.3;III. General Features of Mitochondrial
Bivalent Cation Transport;127
10.4;IV. Transport Sequence of Bivalent Cations across the Mitochondrial Membrane;141
10.5;V. Specificity of the Bivalent Cation Uptake;161
10.6;VI. Attempts to Isolate Components of the Me2+ Transporting Systems;174
10.7;VII. Models of Bivalent Cation Transport in Mitochondria;177
10.8;Acknowledgments;188
10.9;References;188
11;Chapter 4. Role of Subunits in Proton-Translocating ATPase
(F0-F1);198
11.1;I. An Overview of Proton-Translocating ATPase;198
11.2;II. Coupling Factor 1 (Ft) Portion of the Complex;200
11.3;III. Isolation of Individual Subunits and Reconstitution of
F1;211
11.4;IV. Subunits of the F0 Portion and Other Factors of the Proton-Translocating ATPase;218
11.5;V. Genetic Studies on Proton-Translocating ATPase;221
11.6;VI. Conclusion;225
11.7;References;226
12;Chapter 5. Control of Mitochondrial Substrate Oxidation;234
12.1;I. Introduction;234
12.2;II. Respiratory Control—Control of Hydrogen Transfer
by the Phosphorylation Potential;235
12.3;III. Control of the Tricarboxylate Cycle;252
12.4;IV. Control of Pyruvate Dehydrogenase Activity;277
12.5;V. Some Concluding Remarks;286
12.6;Acknowledgments;290
12.7;References;290
13;Chapter 6. Electrochemistry of Nitrogenase and the Role of ATP;296
13.1;I. Introduction;296
13.2;II. Nitrogenase and the Nitrogenase Reaction;297
13.3;III. Oxidation-Reduction of Nitrogenase Components;299
13.4;IV. Model for Nitrogenase-Catalyzed Electron Transfer;305
13.5;References;306
14;Index;310



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