| Preface to the Series | p. ix |
| Preface | p. xiii |
| List of Contributors | p. xv |
| Nitrogen Fixation: An Historical Perspective | p. 1 |
| Introduction | p. 1 |
| When Did Biological Nitrogen Fixation Appear? | p. 3 |
| Nitrogen Fixation and Agriculture | p. 5 |
| Do Plants Assimilate Nitrogen from the Air? | p. 7 |
| Are Bacteria Responsible for Assimilating Nitrogen from the Air? | p. 9 |
| Do Free-Living Rhizobia Fix N[subscript 2]? | p. 12 |
| Commercial Application of Biological Nitrogen Fixation | p. 13 |
| Commercial Application of Industrial Nitrogen Fixation | p. 14 |
| Inorganic Ions and Nitrogen Fixation | p. 15 |
| Methods Used for the Detection of Nitrogen Fixation | p. 16 |
| Beginning of the Biochemistry of Biological Nitrogen Fixation | p. 18 |
| Cell-free Extracts and Beyond | p. 24 |
| Acknowledgement | p. 24 |
| References | p. 26 |
| Haber-Bosch and Other Industrial Processes | p. 33 |
| Background to Industrial Fixation | p. 33 |
| Dinitrogen Chemistry up to ca. 1900 | p. 34 |
| Industrial Fixation of Nitrogen | p. 39 |
| Developments since ca. 1920 | p. 48 |
| Possible Future Developments | p. 52 |
| References | p. 53 |
| Assay Methods for Products of Nitrogenase Action on Substrates | p. 55 |
| Introduction | p. 55 |
| Protons | p. 56 |
| HD Formation | p. 56 |
| Nitrogenous Substrates | p. 57 |
| Carbon-containing Substrates | p. 63 |
| Substrates containing Nitrogen and Carbon | p. 66 |
| Sulfur-containing Substrates | p. 70 |
| Other Assay Components | p. 71 |
| Concluding Remarks | p. 73 |
| References | p. 73 |
| The Structures of the Nitrogenase Proteins and Stabilized Complexes | p. 77 |
| Introduction | p. 77 |
| The Fe Protein | p. 77 |
| The MoFe Protein | p. 81 |
| Nitrogenase Complex Structures | p. 87 |
| Acknowledgements | p. 93 |
| References | p. 93 |
| The Mechanism of Mo-dependent Nitrogenase: Thermodynamics and Kinetics | p. 97 |
| Introduction | p. 97 |
| The Fe-protein Cycle | p. 102 |
| The MoFe-protein Cycle | p. 115 |
| Future Prospects | p. 132 |
| References | p. 133 |
| Strategies for the Functional Analysis of the Azotobacter vinelandii MoFe Protein and its Active Site FeMo-cofactor | p. 141 |
| Introduction | p. 141 |
| Genetic Manipulation and Biochemical Techniques for the Study of A. vinelandii Nitrogenase | p. 142 |
| Insights gained into Nitrogenase Structure-Function from Genetic and Biochemical Studies | p. 148 |
| Summary and Outlook | p. 155 |
| References | p. 157 |
| Chemical Models, Throretical Calculations, and Reactivity of Isolated Iron-Molybdenum Cofactor | p. 161 |
| Introduction | p. 161 |
| Chemical Models | p. 162 |
| Theoretical Calculations | p. 171 |
| Isolation and Reactivity of the Nitrogenase FeMo-cofactor | p. 181 |
| Summary and Future Prospects | p. 190 |
| References | p. 192 |
| Structural Models for the FeMo-cofactor and the P Clusters | p. 201 |
| Introduction | p. 201 |
| FeMo-cofactor Models | p. 203 |
| The P Cluster | p. 210 |
| Concluding Remarks | p. 214 |
| Acknowledgements | p. 214 |
| References | p. 215 |
| Biosynthesis of Iron-Molybdenum and Iron-Vanadium Cofactors of the nif- and vnf-encoded Nitrogenases | p. 219 |
| Introduction | p. 219 |
| Discovery and Characterization of FeMo-cofactor | p. 219 |
| Structures of FeMo-cofactor and FeV-cofactor and their Sites in the MoFe and VFe Proteins | p. 221 |
| FeMo-cofactor and FeV-cofactor Biosynthesis | p. 223 |
| in vitro FeMo-cofactor Synthesis | p. 224 |
| Role of NifQ | p. 227 |
| Role of NifB | p. 228 |
| Role of NifNE | p. 229 |
| Role NifH | p. 231 |
| NifV and the Role of Homocitrate | p. 235 |
| Role of NifX | p. 238 |
| Role of NifU | p. 239 |
| Role of NifS | p. 240 |
| Role of NifM | p. 240 |
| Roles of NifW and NifZ | p. 241 |
| Non-nif Protein Requirements | p. 241 |
| Role of VnfG | p. 242 |
| Role of Nucleotides and Divalent Metals in FeMo-cofactor Synthesis | p. 243 |
| Model for the Biosynthesis of FeMo-cofactor and FeV-cofactor | p. 243 |
| References | p. 247 |
| Vanadium Nitrogenase | p. 255 |
| Introduction | p. 255 |
| Historical Background | p. 255 |
| Characterization | p. 258 |
| Mechanism | p. 267 |
| Genetics | p. 270 |
| Conclusions | p. 274 |
| References | p. 275 |
| Iron-only Nitrogenase: Exceptional Catalytic, Structural and Spectroscopic Features | p. 281 |
| Introduction | p. 281 |
| Metal Regulation of Nitrogenases | p. 283 |
| Factors Influencing Biosynthesis, Catalytic Activity, and Stability of Fe-nitrogenases | p. 284 |
| Mo- and Fe-nitrogenases: Comparison of Subunit Composition, Amino-acid Sequences and Immuno-reactions | p. 287 |
| Structures of the Iron-Sulfur Clusters in Fe-nitrogenase | p. 290 |
| EPR and Redox Properties of the Rhodobacter FeFe Protein | p. 295 |
| Catalytic Characteristics of Iron-only Nitrogenases | p. 299 |
| Fe-only Nitrogenase: Evolutionary Relic or Important Complementary Enzyme System for Diazotrophic Bacteria? | p. 302 |
| Summary and Outlook | p. 304 |
| Acknowledgements | p. 304 |
| References | p. 304 |
| Superoxide-dependent Nitrogenase | p. 309 |
| Introduction | p. 309 |
| Description of Streptomyces thermoautotrophicus | p. 310 |
| Components of the Superoxide-dependent Nitrogen-Fixing System | p. 311 |
| Reduction of N[subscript 2] and Other Catalyzed reactions | p. 316 |
| Genetics | p. 324 |
| Conclusions and Perspectives | p. 328 |
| References | p. 330 |
| Future Challenges and Prospects | p. 333 |
| Introduction | p. 333 |
| Challenges and Prospects | p. 333 |
| Conclusions | p. 336 |
| References | p. 336 |
| Subject Index | p. 337 |
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