Iron-Sulfur Proteins (eBook)

Cover 1
Contents 6
Chapter 1. Biological and Synthetic [Fe3s4] Clusters 10
I. Introduction 10
II. Historical Perspective 11
III. Occurrence and Function 14
IV. Structures 26
V. Electronic, Magnetic, and Vibrational Properties 30
VI. Cluster Conversions 64
VII. Synthetic Model Compounds 67
VIII. Mixed Metal Clusters 72
IX. Future Directions 81
References 82
Chapter 2. The Structures of Rieske and Rieske-Type Proteins 92
I. Introduction 92
II. Historical Background 93
III. Structural Aspects 94
IV. Spectroscopy 122
V. Electrochemistry 146
VI. Biosynthesis 153
VII. Function 155
VIII. Outlook 160
References 161
Chapter 3. Structure, Function, and Biosynthesis of the Metallosulfur Clusters in Nitrogenases 168
I. Introduction 169
II. The Fe Proteins of Molybdenum Nitrogenase 171
III. The MoFe Proteins 175
IV. Biosynthesis of Molybdenum Nitrogenase 183
V. The Mechanism of Molybdenum Nitrogenase 192
VI. The Alternative Nitrogenases 211
VII. Conclusions and Outlook 220
References 221
Chapter 4. The Search for a ''Prismane'' Fe–S Protein 228
I. Introduction 228
II. Historical Discovery of ''Prismane'' Protein (Now Termed Feps) 230
III. Crystallographic Studies 241
IV. Conclusion and Future Studies 254
References 256
Chapter 5. NMR Spectra of Iron–Sulfur Proteins 260
I. Introduction 260
II. Electron Relaxation Times 261
III. Valence Delocalization 266
IV. Considerations on the Reduction Potential 274
V. Solution Structure 275
VI. Folding 280
VII. Perspectives 285
References 286
Chapter 6. Nickel–Iron–Sulfur Active Sites: Hydrogenase and CO Dehydrogenase 292
I. Introduction 292
II. General Concepts Regarding Nickel and Iron–Sulfur 294
III. Hydrogenase 295
IV. CODH/ACS 314
V. Conclusions 335
References 336
Chapter 7. FeS Centers Involved in Photosynthetic Light Reactions 344
I. Introduction 344
II. 2[4Fe–4S] Proteins 347
III. The Bridging Cluster FX 353
IV. [2Fe–2S] Ferredoxins 353
V. High-Potential Iron–Sulfur Proteins 354
VI. The Rieske Protein 356
VII. Evolutionary Remarks 364
References 365
Chapter 8. Simple and Complex Iron–Sulfur Proteins in Sulfate Reducing Bacteria 370
I. Introduction 370
II. Rubredoxin and Desulforedoxin 371
III. Desulfoferrodoxin 375
IV. Rubrerythrin 376
V. Ferredoxins 379
VI. Fuscoredoxin (Novel Fe–S Cluster) 387
VII. APS Reductase 391
VIII. Pyruvate–Ferredoxin Oxidoreductase 394
IX. Sulfite Reductase 395
X. Hydrogenase 397
XI. Molybdopterin-Containing Enzymes in SRB 404
XII. Concluding Remarks 415
References 420
Chapter 9. Application of EPR spectroscopy to the Structural and Functional Study of Iron–Sulfur Proteins 430
I. Introduction 430
II. EPR Characteristics and Relaxation Properties of the Centers 432
III. Application of EPR to the Structural Study of Iron–Sulfur Proteins 459
IV. Application of EPR to the Functional Study of Iron–Sulfur Centers 483
V. Conclusion 493
Appendix: Spin–Lattice Relaxation Processes 495
References 496
Index 508
Contents of Previous Volumes 520