Catalysts for Nitrogen Fixation: Nitrogenases, Relevant Chemical Models and Commercial Processes by Barry E. SmithCatalysts for Nitrogen Fixation: Nitrogenases, Relevant Chemical Models and Commercial Processes by Barry E. Smith

Catalysts for Nitrogen Fixation: Nitrogenases, Relevant Chemical Models and Commercial Processes

EditorBarry E. Smith, Raymond L. Richards, William E. Newton

Paperback | December 15, 2010

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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.
Title:Catalysts for Nitrogen Fixation: Nitrogenases, Relevant Chemical Models and Commercial ProcessesFormat:PaperbackDimensions:356 pagesPublished:December 15, 2010Publisher:Springer NetherlandsLanguage:English

The following ISBNs are associated with this title:

ISBN - 10:9048166756

ISBN - 13:9789048166756

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Table of Contents

Preface to the Series. Preface. List of Contributors.1: Nitrogen Fixation: An Historical Perspective; K. Fisher and W.E. Newton1. Introduction2. When did Biological Nitrogen Fixation Appear?3. Nitrogen Fixation and Agriculture4. 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 Fixation8. Commercial Application of Industrial Nitrogen Fixation9. Inorganic Ions and Nitrogen Fixation10. Methods Used for the Detection of Nitrogen Fixation11. Beginning of the Biochemistry of Biological Nitrogen Fixation12. Cell-free Extracts and BeyondAcknowledgementReferences2: Haber-Bosch and Other Industrial Processes; G.J. Leigh1. Background to Industrial Fixation2. Dinitrogen Chemistry up to ca. 19003. Industrial Fixation of Nitrogen4. Developments since ca. 19205. Possible Future DevelopmentsReferences3: Assay Methods for Products of Nitrogenase Action on Substrates; M.J. Dilworth1. Introduction2. Protons3. HD Formation4. Nitrogenous Substrates5. Carbon-containing Substrates6. Substrates containing Nitrogen and Carbon7. Sulfur-containing Substrates8. Other Assay Components9. Concluding RemarksReferences4: The Structures of the Nitrogenase Proteins and Stabilized Complexes; P.M.C. Benton and J.W. Peters1. Introduction2.The Fe Protein3. The MoFe Protein4. Nitrogenase Complex StructuresAcknowledgementsReferences5: The Mechanism of Mo-dependent Nitrogenase: Thermodynamics and Kinetics; R.Y. Igarashi and L.C. Seefeldt1. Introduction2. The Fe-protein Cycle3. The MoFe-protein Cycle4. Future ProspectsReferences6: 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. Dean1. Introduction2. Genetic Manipulation and Biochemical Techniques for the Study of A. vinelandii Nitrogenase3. Insights gained into Nitrogenase Structure-Function from Genetic and Biochemical Studies4. Summary and OutlookReferences7: Chemical Models, Theoretical Calculations, and Reactivity of Isolated Iron-Molybdenum Cofactor; F. Barrière, M.C. Durrant and C.J. Pickett1. Introduction2. Chemical Models3. Theoretical Calculations4. Isolation and Reactivity of the Nitrogenase FeMo-cofactor5. Summary and Future ProspectsReferences8: Structural Models for the FeMo-cofactor and the P Clusters; D.J. Evans1. Introduction2. FeMo-cofactor Models3. The P Cluster4. Concluding RemarksAcknowledgementsReferences9. Biosynthesis of Iron-Molybdenum and Iron-Vanadium Cofactors of the nif- and vnf-encoded Nitrogenases; P.W. Ludden, P. Rangaraj and L.M. Rubio1. Introduction2. Discovery and Characterization of FeMo-cofactor3. Structures of FeMo-cofactor and FeV-cofactor and their Sites in the MoFe and VFe Proteins4. FeMo-cofactor and FeV-cofactor Biosynthesis5. in vitro FeMo-cofactor Synthesis6. Role of NifQ7. Role of NifB8. Role of NifNE9. Role NifH10. NifV and the Role of Homocitrate11. Role of NifX12. Role of NifU13. Role of NifS14. Role of NifM15. Roles of NifW and NifZ16. Non-nif Protein Requirements17. Role of VnfG18. Role of Nucleotides and Divalent Metals in FeMo-cofactor Synthesis19. Model for the Biosynthesis of FeMo-cofactor and FeV-cofactorReferences10: Vanadium Nitrogenase; B.J. Hales1. Introduction2. Historical Background3. Characterization4. Mechanism5. Genetics6. ConclusionsReferences11. Iron-only Nitrogenase: Exceptional Catalytic, Structural and Spectroscopic Features; K. Schneider and A. Müller1. Introduction2. Metal Regulation of Nitrogenases3. Factors Influencing Biosynthesis, Catalytic Activity, and Stability of Fe-nitrogenases4. Mo- and Fe-nitrogenases: Comparison of Subunit Composition, Amino-acid Sequences and Immuno-reactions5. Structures of the Iron-Sulfur Clusters in Fe-nitrogenase6. EPR and Redox Properties of the Rhodobacter FeFe Protein7. Catalytic Characteristics of Iron-only Nitrogenases8. Fe-only Nitrogenase: Evolutionary Relic or Important Complementary Enzyme System for Diazotrophic Bacteria?9. Summary and OutlookAcknowledgementsReferences12: Superoxide-dependent Nitrogenase; D. Gadkari1. Introduction2. Description of Streptomyces thermoautotrophicus3. Components of the Superoxide-dependent Nitrogen-Fixing System4. Reduction of N2 and Other Catalyzed reactions5. Genetics6. Conclusions and PerspectivesReferences13: Future Challenges and Prospects; R.L. Richards and B.E. Smith1. Introduction 2. Challenges and Prospects3. ConclusionsReferencesSubject Index.