| Preface to the Series |
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ix | |
| Preface |
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xiii | |
| List of Contributors |
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xv | |
| Chapter 1. Nitrogen Fixation: An Historical Perspective |
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K. Fisher and W.E. Newton |
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1 | (32) |
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1 | (2) |
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2. When Did Biological Nitrogen Fixation Appear? |
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3 | (2) |
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3. Nitrogen Fixation and Agriculture |
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5 | (2) |
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4. Do Plants Assimilate Nitrogen from the Air? |
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7 | (2) |
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5. Are Bacteria Responsible for Assimilating Nitrogen from the Air? |
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9 | (3) |
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6. Do Free-Living Rhizobia Fix N2? |
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12 | (1) |
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7. Commercial Application of Biological Nitrogen Fixation |
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13 | (1) |
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8. Commercial Application of Industrial Nitrogen Fixation |
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14 | (1) |
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9. Inorganic Ions and Nitrogen Fixation |
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15 | (1) |
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10. Methods Used for the Detection of Nitrogen Fixation |
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16 | (2) |
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11. Beginning of the Biochemistry of Biological Nitrogen Fixation |
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18 | (6) |
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12. Cell-free Extracts and Beyond |
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24 | (1) |
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24 | (2) |
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26 | (7) |
| Chapter 2. Haber-Bosch and Other Industrial Processes |
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33 | (22) |
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1. Background to Industrial Fixation |
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33 | (1) |
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2. Dinitrogen Chemistry up to ca. 1900 |
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34 | (5) |
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3. Industrial Fixation of Nitrogen |
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39 | (9) |
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4. Developments since ca. 1920 |
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48 | (4) |
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5. Possible Future Developments |
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52 | (1) |
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53 | (2) |
| Chapter 3. Assay Methods for Products of Nitrogenase Action on Substrates |
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55 | (22) |
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55 | (1) |
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56 | (1) |
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56 | (1) |
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4. Nitrogenous Substrates |
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57 | (6) |
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5. Carbon-containing Substrates |
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63 | (3) |
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6. Substrates containing Nitrogen and Carbon |
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66 | (4) |
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7. Sulfur-containing Substrates |
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70 | (1) |
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8. Other Assay Components |
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71 | (2) |
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73 | (1) |
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73 | (4) |
| Chapter 4. The Structures of the Nitrogenase Proteins and Stabilized Complexes |
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P.M.C. Benton and J.W. Peters |
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77 | (20) |
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77 | (1) |
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77 | (4) |
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81 | (6) |
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4. Nitrogenase Complex Structures |
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87 | (6) |
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93 | (1) |
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93 | (4) |
| Chapter 5. The Mechanism of Mo-dependent Nitrogenase: Thermodynamics and Kinetics |
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R.Y. Igarashi and L.C. Seefeldt |
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97 | (44) |
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97 | (5) |
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102 | (13) |
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3. The MoFe-protein Cycle |
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115 | (17) |
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132 | (1) |
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133 | (8) |
| Chapter 6. Strategies for the Functional Analysis of the Azotobacter vinelandii MoFe Protein and its Active Site FeMo-cofactor |
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S.M. Mayer, P.C. Dos Santos, L.C. Seefeldt and D.R. Dean |
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141 | (20) |
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141 | (1) |
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2. Genetic Manipulation and Biochemical Techniques for the Study of A. vinelandii Nitrogenase |
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142 | (6) |
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3. Insights gained into Nitrogenase Structure-Function from Genetic and Biochemical Studies |
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148 | (7) |
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155 | (2) |
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157 | (4) |
| Chapter 7. Chemical Models, Throretical Calculations, and Reactivity of Isolated Iron-Molybdenum Cofactor |
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F. Barriere, M.C. Durrant and C.J. Pickett |
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161 | (40) |
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161 | (1) |
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162 | (9) |
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3. Theoretical Calculations |
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171 | (10) |
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4. Isolation and Reactivity of the Nitrogenase FeMo-cofactor |
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181 | (9) |
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5. Summary and Future Prospects |
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190 | (2) |
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192 | (9) |
| Chapter 8. Structural Models for the FeMo-cofactor and the P Clusters |
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201 | (18) |
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201 | (2) |
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203 | (7) |
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210 | (4) |
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214 | (1) |
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214 | (1) |
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215 | (4) |
| Chapter 9. Biosynthesis of Iron-Molybdenum and Iron-Vanadium Cofactors of the nif- and vnf-encoded Nitrogenases |
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P.W. Ludden, P. Rangaraj and L.M. Rubio |
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219 | (36) |
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219 | (1) |
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2. Discovery and Characterization of FeMo-cofactor |
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219 | (2) |
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3. Structures of FeMo-cofactor and FeV-cofactor and their Sites in the MoFe and VFe Proteins |
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221 | (2) |
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4. FeMo-cofactor and FeV-cofactor Biosynthesis |
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223 | (1) |
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5. in vitro FeMo-cofactor Synthesis |
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224 | (3) |
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227 | (1) |
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228 | (1) |
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229 | (2) |
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231 | (4) |
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10. NifV and the Role of Homocitrate |
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235 | (3) |
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238 | (1) |
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239 | (1) |
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240 | (1) |
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240 | (1) |
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15. Roles of NifW and NifZ |
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241 | (1) |
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16. Non-nif Protein Requirements |
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241 | (1) |
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242 | (1) |
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18. Role of Nucleotides and Divalent Metals in FeMo-cofactor Synthesis |
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243 | (1) |
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19. Model for the Biosynthesis of FeMo-cofactor and FeV-cofactor |
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243 | (4) |
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247 | (8) |
| Chapter 10. Vanadium Nitrogenase |
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255 | (26) |
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255 | (1) |
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255 | (3) |
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258 | (9) |
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267 | (3) |
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270 | (4) |
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274 | (1) |
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275 | (6) |
| Chapter 11. Iron-only Nitrogenase: Exceptional Catalytic, Structural and Spectroscopic Features |
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K. Schneider and A. Müller |
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281 | (28) |
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281 | (2) |
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2. Metal Regulation of Nitrogenases |
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283 | (1) |
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3. Factors Influencing Biosynthesis, Catalytic Activity, and Stability of Fe-nitrogenases |
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284 | (3) |
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4. Mo- and Fe-nitrogenases: Comparison of Subunit Composition, Amino-acid Sequences and Immuno-reactions |
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287 | (3) |
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5. Structures of the Iron-Sulfur Clusters in Fe-nitrogenase |
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290 | (5) |
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6. EPR and Redox Properties of the Rhodobacter FeFe Protein |
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295 | (4) |
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7. Catalytic Characteristics of Iron-only Nitrogenases |
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299 | (3) |
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8. Fe-only Nitrogenase: Evolutionary Relic or Important Complementary Enzyme System for Diazotrophic Bacteria'? |
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302 | (2) |
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304 | (1) |
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304 | (1) |
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304 | (5) |
| Chapter 12. Superoxide-dependent Nitrogenase |
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309 | (24) |
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309 | (1) |
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2. Description of Streptomyces thermoautotrophicus |
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310 | (1) |
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3. Components of the Superoxide-dependent Nitrogen-Fixing System |
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311 | (5) |
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4. Reduction of N2 and Other Catalyzed reactions |
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316 | (8) |
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324 | (4) |
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6. Conclusions and Perspectives |
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328 | (2) |
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330 | (3) |
| Chapter 13. Future Challenges and Prospects |
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R.L. Richards and B.E. Smith |
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333 | (4) |
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333 | (1) |
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2. Challenges and Prospects |
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333 | (3) |
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336 | (1) |
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336 | (1) |
| Subject Index |
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337 | |