Structure and Metabolic Mechanisms - 1st Edition - ISBN: 9780124560031, 9780323149525

Structure and Metabolic Mechanisms

1st Edition

Editors: Walter Lovenberg
eBook ISBN: 9780323149525
Imprint: Academic Press
Published Date: 1st January 1977
Page Count: 460
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Iron-Sulfur Proteins, Volume III: Structure and Metabolic Mechanisms focuses on numerous advances that have been made in the vital role of iron-sulfur proteins in biological processes. Of the 10 chapters in this book, five chapters present advances in biochemical areas and the other five chapters discuss some of the elegant physical studies made.

This book begins with a description of the nitrogenase gene and the molecular mechanism of this complex enzyme. It then centers on the role of iron-sulfur proteins in mammalian mitochondrial function, as well as on the mechanism of biosynthesis and the function of these proteins in formate metabolism. Different approaches that have yielded advances in the understanding of the iron-sulfur clusters are also shown. This book also gives an in-depth discussion on the theoretical aspects of the redox properties of iron-sulfur proteins.

Table of Contents

List of Contributors


Contents of Other Volumes

1. Nitrogenase-Derepressed Mutants of Klebsiella pneumoniae

I. Introduction

II. Glutamine Synthetase as Regulatory Protein

III. Nitrogenase-Derepressed Mutants

IV. Discussion and Summary


2. Current Topics and Problems in the Enzymology of Nitrogenase

I. Introduction

II. Composition and Structure of Nitrogenase Protein Components

III. Interaction of MgATP and the Fe Protein

IV. Sequence of Electron Transfers between Nitrogenase Components

V. Structural and Mechanistic Hypotheses


3. Iron-Sulfur Centers of the Mitochondrial Electron Transfer System—Recent Developments

I. Introduction

II. Iron-Sulfur Centers of the Mitochondrial Electron Transfer System

III. Relation of Iron-Sulfur Centers to Energy Conservation

IV. Outlook


4. Biosynthesis of Iron-Sulfur Proteins

I. Introduction

II. Bacterial Protein Synthesis

III. Regulation of Synthesis of Ferredoxin

IV. Conversion of Apoferredoxin to Holo- or Native Ferredoxin

V. Synthesis of Specific Proteins in Vitro

VI. Immunological Studies with Clostridial Ferredoxin

VII. Enzymatic Assays for Ferredoxin

VIII. Synthesis of Clostridial Ferredoxin or Apoferredoxin in Vitro


5. Role of Iron-Sulfur Proteins in Formate Metabolism

I. Introduction

II. Role of Formate in Metabolism

III. Ferredoxin and Formate Metabolism

IV. Formate Dehydrogenases and Formate Metabolism

V. Concluding Remarks


6. X-Ray Analysis of High-Potential Iron-Sulfur Proteins and Ferredoxins

I. Introduction

II. Fe4S4 Active Centers and the Three-State Hypothesis

III. Comparison of the Protein-Bound and Synthetic Fe4S4

IV. Characteristic Features of the Cluster Binding Cavities

V. Analysis of Reduced versus Oxidized HiPIP

VI. Conclusions and Review


7. Synthetic Analogues of the Active Sites of Iron-Sulfur Proteins

I. Introduction

II. Synthesis and Structures of 1-Fe, 2-Fe, and 4-Fe Active-Site Analogues

III. Physical Properties of Analogues

IV. Chemical Reactivity of Analogues

V. Iron-Sulfur Units as Redox Centers

VI. Perspectives and Conclusions


8. Evidence from Mössbauer Spectroscopy and Magnetic Resonance on the Active Centers of the Iron-Sulfur Proteins

I. Introduction

II. Spectroscopy of the Active Center

III. Proteins with 1 Fe Centers

IV. Proteins with 2 Fe-2 S Centers

V. Proteins with 4 Fe-4 S

VI. Conclusions


9. Redox Mechanisms of Iron-Sulfur Proteins

I. Introduction

II. Recent Development in Simple Redox Chemistry

III. Redox Dynamics of Structurally Characterized Iron-Sulfur Proteins

IV. Survey of the Redox Behavior of Structurally Less Characterized Iron-Sulfur Proteins


10. Recent Mössbauer Results of Some Iron-Sulfur Proteins and Model Complexes

I. Introduction

II. Rubredoxin

III. The MoFe Protein of Nitrogenase

IV. Model Compounds for Rubredoxin and 4 Fe-4 S* Clusters


Author Index

Subject Index


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© Academic Press 1977
Academic Press
eBook ISBN:

About the Editor

Walter Lovenberg

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