Catalysts for nitrogen fixation : nitrogenases, relevant chemical models, and commercial processes

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書誌事項

Catalysts for nitrogen fixation : nitrogenases, relevant chemical models, and commercial processes

edited by Barry E. Smith, Raymond L. Richards, William E. Newton

（Nitrogen fixation : origins, applications, and research progress, v. 1）

Kluwer Academic Publishers, 2004

大学図書館所蔵 件 / 全7件

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注記

Includes bibliographical references and index

内容説明・目次

内容説明

Biological nitrogen fixation provides more than 50% of the total annual input of the essential element nitrogen to world agriculture. Thus, it is of immense agronomic importance and critical to food supplies, particularly in developing countries. This book, with chapters authored by internationally renowned experts, provides a comprehensive and detailed account of the fascinating history of the process - including the surprising discoveries of molybdenum-independent nitrogenases and superoxide-dependent nitrogenase; a review of Man's attempts to emulate the biological process - most successfully with the commercially dominant Haber-Bosch process; and the current state of the understanding art with respect to the enzymes - called nitrogenases - responsible for biological nitrogen fixation. The initial chapters use a historical approach to the biological and industrial processes, followed by an overview of assay methodologies. The next set of chapters focuses on the classical enzyme, the molybdenum nitrogenase, and details its biosynthesis, structure, composition, and mechanism of action as well as detailing both how variants of its two component proteins are constructed by recombinant DNA technology and how computational techniques are being applied. The sophisticated chemical modelling of the metal-containing clusters in the enzyme is reviewed next, followed by a description of the two molybdenum-independent nitrogenases - first, the vanadium-containing enzyme and then the iron-only nitrogenase - together with some thoughts as to why they exist! Then follows an up-to-date treatment of the clearly "non-classical" properties of the superoxide-dependent nitrogenase, which more closely resembles molybdenum-containing hydroxylases and related enzymes, like nitrate reductase, that it does the other nitrogenases. Each chapter contains an extensive list of references. This book is the self-contained first volume of a comprehensive seven-volume series. No other available work provides the up-to-date and in-depth coverage of this series and this volume. This book is intended to serve as an indispensable reference work for all scientists working in this area, including agriculture and the closely related metals-in-biology area; to assist students to enter this challenging area of research; and to provide science administrators easy access to vital relevant information.

目次

  • Preface to the Series. Preface. List of Contributors. 1: Nitrogen Fixation: An Historical Perspective
  • K. Fisher and W.E. Newton 1. Introduction 2. When did Biological Nitrogen Fixation Appear? 3. Nitrogen Fixation and Agriculture 4. Do Plants Assimilate Nitrogen from the Air? 5. Are Bacteria Responsible for Assimilating Nitrogen from the Air? 6. Do Free-Living Rhizobia Fix N2? 7. Commercial Application of Biological Nitrogen Fixation 8. Commercial Application of Industrial Nitrogen Fixation 9. Inorganic Ions and Nitrogen Fixation 10. Methods Used for the Detection of Nitrogen Fixation 11. Beginning of the Biochemistry of Biological Nitrogen Fixation 12. Cell-free Extracts and Beyond Acknowledgement References 2: Haber-Bosch and Other Industrial Processes
  • G.J. Leigh 1. Background to Industrial Fixation 2. Dinitrogen Chemistry up to ca. 1900 3. Industrial Fixation of Nitrogen 4. Developments since ca. 1920 5. Possible Future Developments References 3: Assay Methods for Products of Nitrogenase Action on Substrates
  • M.J. Dilworth 1. Introduction 2. Protons 3. HD Formation 4. Nitrogenous Substrates 5. Carbon-containing Substrates 6. Substrates containing Nitrogen and Carbon 7. Sulfur-containing Substrates 8. Other Assay Components 9. Concluding Remarks References 4: The Structures of the Nitrogenase Proteins and Stabilized Complexes
  • P.M.C. Benton and J.W. Peters 1. Introduction 2.The Fe Protein 3. The MoFe Protein 4. Nitrogenase Complex Structures Acknowledgements References 5: The Mechanism of Mo-dependent Nitrogenase: Thermodynamics and Kinetics
  • R.Y. Igarashi and L.C. Seefeldt 1. Introduction 2. The Fe-protein Cycle 3. The MoFe-protein Cycle 4. Future Prospects References 6: Strategies for the Functional Analysis of the Azotobacter vinelandii MoFe Protein and its Active Site FeMo-cofactor
  • S.M. Mayer, P.C. Dos Santos, L.C. Seefeldt and D.R. Dean 1. Introduction 2. Genetic Manipulation and Biochemical Techniques for the Study of A. vinelandii Nitrogenase 3. Insights gained into Nitrogenase Structure-Function from Genetic and Biochemical Studies 4. Summary and Outlook References 7: Chemical Models, Theoretical Calculations, and Reactivity of Isolated Iron-Molybdenum Cofactor
  • F. Barriere, M.C. Durrant and C.J. Pickett 1. Introduction 2. Chemical Models 3. Theoretical Calculations 4. Isolation and Reactivity of the Nitrogenase FeMo-cofactor 5. Summary and Future Prospects References 8: Structural Models for the FeMo-cofactor and the P Clusters
  • D.J. Evans 1. Introduction 2. FeMo-cofactor Models 3. The P Cluster 4. Concluding Remarks Acknowledgements References 9. Biosynthesis of Iron-Molybdenum and Iron-Vanadium Cofactors of the nif- and vnf-encoded Nitrogenases
  • P.W. Ludden, P. Rangaraj and L.M. Rubio 1. Introduction 2. Discovery and Characterization of FeMo-cofactor 3. Structures of FeMo-cofactor and FeV-cofactor and their Sites in the MoFe and VFe Proteins 4. FeMo-cofactor and FeV-cofactor Biosynthesis 5. in vitro FeMo-cofactor Synthesis 6. Role of NifQ 7. Role of NifB 8. Role of NifNE 9. Role NifH 10. NifV and the Role of Homocitrate 11. Role of NifX 12. Role of NifU 13. Role of NifS 14. Role of NifM 15. Roles of NifW and NifZ 16. Non-nif Protein Requirements 17. Role of VnfG 18. Role of Nucleotides and Divalent Metals in FeMo-cofactor Synthesis 19. Model for the Biosynthesis of FeMo-cofactor and FeV-cofactor References 10: Vanadium

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