Molecular Properties V2

1st Edition - December 2, 2012
Imprint: Academic Press
Editor: Walter Lovenberg
Language: English
Hardback ISBN:
9 7 8 - 0 - 1 2 - 4 5 6 0 0 2 - 4
Paperback ISBN:
9 7 8 - 0 - 1 2 - 4 3 1 6 2 6 - 3
eBook ISBN:
9 7 8 - 0 - 3 2 3 - 1 5 4 2 9 - 1

Molecular Properties, Volume II is a collection of papers that deals with the physical and chemical properties of iron-sulfur proteins, with emphasis on the theory and application… Read more

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Molecular Properties, Volume II is a collection of papers that deals with the physical and chemical properties of iron-sulfur proteins, with emphasis on the theory and application of physicochemical techniques related to metalloproteins. One paper describes the chemical properties of simple iron-sulfur proteins focusing on chloroplast, bacterial-type ferredoxins, and the nature of the active site in the ferredoxins. Another paper notes that rubredoxin sequences can offer phylogenetic, evolutionary, or genetic data. The paper shows that rubredoxins from aerobic and anaerobic bacteria have originated from some common ancestor. One paper analyzes the chemical and physical properties of rubredoxin and the way they relate to the structure resulting from an X-ray diffraction. The investigator can use electron paramagnetic resonance (EPR), electron nuclear double resonance (ENDOR) spectroscopy, or nuclear magnetic resonance (NMR) to determine the structural and functional features of simple and conjugated iron-sulfur proteins. He can also use a proton magnetic resonance (PMR) spectroscopy to study the structures and interactions of proteins in solution, such as ribonuclease, lysozyme, and the heme proteins (hemoglobins or myoglobins). Cellular biologists, micro-biologists, bio-chemists, and scientists involved in biological systems research will find this collection very informative.

List of Contributors

Preface

Contents of Volume I

1. The Chemical Properties of Ferredoxins

I. Introduction

II. Chemical Characteristics of Ferredoxins

III. The Chemical Reactivity of Ferredoxins

IV. Reconstitution Studies with Ferredoxins

References

2. The Types, Distribution in Nature, Structure-Function, and Evolutionary Data of the Iron-Sulfur Proteins

I. Introduction

II. The Primary Structures of the Iron-Sulfur Proteins

III. A Consideration of the Individual Iron-Sulfur Proteins

IV. Algal and Plant Ferredoxins

V. Putidaredoxin

VI. Adrenodoxin and Testerodoxin

VII. High-Potential Iron Protein (HIPIP)

VIII. Euglena Iron-Sulfur Protein

IX. Azotobacter Iron-Sulfur Proteins, I, II, and III

X. Iron-Sulfur Protein from Complex III of Mitochondria

XI. Clostridium Pasteurianum Nitrogenase

XII. Bacillus Polymyxa Ferredoxin and the Bacteroid Iron-Sulfur Protein

XIII. Type II Iron-Sulfur Proteins, Flavodoxins, Immunochemistry, and Synthesis of Iron-Sulfur Proteins

XIV. Evolution

XV. Summary

XVI. Appendix: Distribution and Some Properties of Nonheme Iron Proteins

References

3. The Iron-Sulfur Complex in Rubredoxin

I. Introduction

II. Chemical Properties

III. Stereochemistry and Electronic Structure

IV. Summary and Conclusions

References

4. Crystal and Molecular Structure of Rubredoxin from Clostridium Pasteurianum

I. Theory

II. Experimental Procedure

III. Determination of the Structure

IV. Addendum

References

5. Probing Iron-Sulfur Proteins with EPR and ENDOR Spectroscopy

I. Introduction

II. The EPR Phenomenon

III. The Phenomenon of ENDOR

IV. The Physics of Iron in Proteins

V. Rubredoxins

VI. Two-Iron (Plant-Type) Ferredoxins

VII. Iron-Sulfur Proteins with Four Iron Atoms

VIII. Eight-Iron (Clostridial-Type) Ferredoxins

IX. EPR in More Complex Iron-Sulfur Proteins

References

6. Mössbauer Spectroscopy of Iron-Sulfur Proteins

I. The Mössbauer Spectroscopic Method

II. Mössbauer Data

References

7. NMR Spectroscopy of the Iron-Sulfur Proteins

I. Introduction

II. Paramagnetism and NMR

III. Rubredoxin

IV. Eight-Iron Ferredoxins

V. High-Potential Iron Protein

VI. A Synthetic Analogue of the Fe4S4 Clusters

VII. 13C NMR Studies of C. Acidi-Urici Ferredoxin

VIII. Two-Iron Ferredoxins

IX. Validity of the PMR Results

References

8. Current Insights into the Active Center of Spinach Ferredoxin and Other Iron-Sulfur Proteins

I. Exchange Interaction and Antiferromagnetic Coupling

II. Consequences of the Exchange Interaction

III. Physical Data

IV. Optical Spectra

V. Chemical Data

VI. The Structure of the Active Center

VII. The Relationship between the Structure of Spinach Ferredoxin and Other 2 Fe-S* Proteins

VIII. The Properties of the 4 Fe-S* Iron-Sulfur Proteins

IX. Properties of the 8 Fe-S* Iron-Sulfur Proteins

X. Conclusions

References

Author Index

Subject Index

Life Sciences

Physical Sciences & Engineering

Social Sciences & Humanities

Health

Molecular Properties V2

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