Current Topics in Bioenergetics

List of Contributors

Preface

Contents of Previous Volumes

Proton-ATPase of Chloroplasts

I. Introduction

II. Resolution and Reconstitution of Chloroplast Membranes

III. Isolation and Properties of the Chloroplast Coupling Device (CF0-CF1)

IV. Structure and Function of Purified CF1

V. Subunit Structure of CF1 and Partial Resolution of the Enzyme into Active Units

VI. Structure and Function of the Membrane Sector of the Coupling Device (CF0)

VII. Conformational Changes, Chemical Modification, and Nucleotide Binding in Membrane-Bound CF1

VIII. Suggested Mechanisms for Proton Motive Force-Driven ATP Formation

References

Biochemistry and Genetics of Bacterial H+-Translocating ATPases

I. Perspective

II. Distribution and Function of Bacterial H+-ATPase

III. The Extrinsic F1-ATPase of Bacteria

IV. Purification and Properties of F1F0-ATPase Complexes

V. Isolation and Reconstitution of F0

VI. Genetics of Escherichia coli H+-ATPase

VII. Summary and Prospects

References

Proton-Linked Transport in Chromaffin Granules

I. The Legacy of the Adrenal Medulla

II. An Integrated View of Chromaffin-Granule Functions

III. Chromaffin-Granule Matrix

IV. Chromaffin-Granule Membrane

V. ATP-Dependent Proton Translocation

VI. Catecholamine Transport

VII. Uptake of Other Ions

VIII. Redox Elements

IX. Bioenergetic Processes in Other Secretory Vesicles

References

Note Added in Proof

Regulation of the Synthesis and Hydrolysis of ATP in Biological Systems: Role of Peptide Inhibitors of H+-ATPases

I. Introduction

II. Purification

III. Physicochemical Properties

IV. Relationship to F1 Subunits

V. Possibility of Multiple Forms

VI. Localization Relative to F0: Role of Lipids

VII. Requirements for Optimal Interaction with F1

VIII. Effect of the Kinetics of ATP Hydrolysis and the Reactivity of Amino Acid Residues at the Hydrolytic Site(s) of F1

IX. Effect on Nucleotide Binding to F1

X. Effect of Energy-Linked Activities—Some Facts and Some Models

XI. Specificity and Cross-Reactivities

XII. Similarity in Mode of Action to AMP-PNP

XIII. Opposing Action of Aurovertin

XIV. Factor A, a Peptide Inhibitor-Free Form of F1 That "Couples"

XV. Possible Role in Regulating Calcium Uptake

XVI. Presence in Tumor Mitochondria

XVII. Biosynthesis

XVIII. Comparison with Other Protein Inhibitors

XIX. Summary—What We Have Not Learned So Far

References

Structure and Mechanism of the (Na,K)-ATPase

I. Introduction

II. Purification and Reconstitution

III. Structure

IV. Mechanism

V. Comparisons with Other ATPases

VI. Conclusion

References

Actomyosin ATPase and Muscle Contraction

I. Introduction

II. Kinetics of the Crossbridge Cycle in Solution

III. Kinetics of the Crossbridge Cycle in Muscle

IV. Comparison of the Ca2+ Pump ATPase and Actomyosin ATPase

V. Summary

References

Index