Bibliographic Information

Biological properties

edited by Walter Lovenberg

(Molecular biology : an international series of monographs and textbooks, . Iron-sulfur proteins ; v. 1)

Academic Press, 1973

Available at  / 27 libraries

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Includes bibliographies and indexes

Description and Table of Contents

Description

Biological Properties is a collection of papers that deals with the biological properties of iron-sulfur proteins. One paper reviews the role of electron paramagnetic resonance in forwarding knowledge about iron-sulfur proteins. Iron-sulfur proteins are iron proteins where sulfur is a ligand of the iron, of which the iron is not simultaneously held by a stronger ligand such as porphyrin. Another paper discusses the role of bacterial ferredoxins in coupled oxidation-reduction reactions, the role of hydrogenase in oxidation-reduction, as well as the bacterial iron-sulfur proteins, such as azoferredoxin and molybdoferredoxin. Abiological models of nitrogenase involve molybdenum and iron with sulfur ligands; these abiological systems can be the first models that show the biological activity of iron-sulfur enzymes which these systems try to copy. One paper investigates the role of iron-sulfur proteins in photosynthesis, particularly the photoreduction of ferrodoxin, the mechanism of NADPH formation, and the possible role of ferrodoxin in cyclic photophosphorylation. This collection is suitable for bio-chemists, cellular biologists, micro-biologists, and scientists involved in research in the biological disciplines.

Table of Contents

List of Contributors Preface Contents of Volume II 1. Development of the Field and Nomenclature I. Introduction II. Occurrence of Iron in Living Matter III. Development of the Field of Iron-Sulfur Proteins IV. Function of Iron-Sulfur Proteins V. Nomenclature References 2. Bacterial Ferredoxins and/or Iron-Sulfur Proteins as Electron Carriers I. Introduction II. Demonstration of Ferredoxin-Requiring Reactions III. Purification of Ferredoxin IV. Reactions That Require Ferredoxin V. Number of Electrons Carried by Ferredoxins VI. High Molecular Weight Iron-Sulfur Proteins Involved in Electron Transport VII. Hydrogenase VIII. Nitrogenase: A Complex of Two Iron-Sulfur Proteins References 3. Comparative Biochemistry of Iron-Sulfur Proteins and Dinitrogen Fixation I. Relationship of Iron-Sulfur Proteins and Dinitrogen Fixation II. Definition of Nitrogenase III. Iron-Sulfur Proteins as Reductants for Nitrogenase IV. Extraction, Fractionation, and Purification of Nitrogenase V. Characteristics of Nitrogenase and Its Components VI. Metals and Biological Dinitrogen Fixation VII. Abiological Dinitrogen Fixation by Iron and Sulfur References 4. Iron-Sulfur Proteins in Photosynthesis I. Ferredoxin Reduction II. Ferredoxin Catalytic Activity III. Photosynthetic and Oxidative Energy Transduction References 5. Ferredoxin and Carbon Assimilation I. Introduction II. Reductive Carboxylic Acid Cycle of Bacterial Photosynthesis III. Reductive Monocarboxylic Acid Cycle of Fermentative Metabolism IV. Enzymes Catalyzing Ferredoxin-Dependent Carboxylation Reactions V. Concluding Remarks References 6. Structure and Reactions of a Microbial Monoxygenase: The Role of Putidaredoxin I. Introduction II. Putidaredoxin-Structural Properties III. Putidaredoxin-Cytochrome P-450cam Interactions IV. Progress and Problems References 7. Role of Rubredoxin in Fatty Acid and Hydrocarbon Hydroxylation Reactions I. Biological Utilization of Hydrocarbons II. Rubredoxin and Other Components of a Bacterial Enzyme System Catalyzing Hydrocarbon and Fatty Acid Hydroxylation III. Characterization of Rubredoxin from P. Oleovorans IV. Activity of Iron-Sulfur Proteins as Electron Carriers in ?-Hydroxylation V. Activity of P. Oleovorans Rubredoxin in Reduction of Alkyl Hydroperoxides VI. Summary References 8. Adrenodoxin: An Iron-Sulfur Protein of Adrenal Cortex Mitochondria I. Introduction II. Physical Properties of Adrenodoxin III. The Biological Function of Adrenodoxin IV. Conclusion References 9. Iron-Sulfur Flavoprotein Dehydrogenases I. Introduction II. Succinate Dehydrogenase III. Mammalian NADH Dehydrogenase IV. Dihydroorotate Dehydrogenase References 10. Iron-Sulfur Flavoprotein Hydroxylases I. General Introduction II. Xanthine Oxidase III. Aldehyde Oxidase References Author Index Subject Index

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Details

  • NCID
    BA06632168
  • ISBN
    • 0124560016
  • LCCN
    72013613
  • Country Code
    us
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    New York ; London
  • Pages/Volumes
    xiii, 385 p.
  • Size
    24 cm
  • Parent Bibliography ID
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