Iron-Sulfur Proteins

Cammack, Richard

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Table of contents
  • Contentsv
  • Chapter 1. Biological and Synthetic [Fe3s4] Clusters1
  • I. Introduction1
  • II. Historical Perspective2
  • III. Occurrence and Function5
  • IV. Structures17
  • V. Electronic, Magnetic, and Vibrational Properties21
  • VI. Cluster Conversions55
  • VII. Synthetic Model Compounds58
  • VIII. Mixed Metal Clusters63
  • IX. Future Directions72
  • References73
  • Chapter 2. The Structures of Rieske and Rieske-Type Proteins83
  • I. Introduction83
  • II. Historical Background84
  • III. Structural Aspects85
  • IV. Spectroscopy113
  • V. Electrochemistry137
  • VI. Biosynthesis144
  • VII. Function146
  • VIII. Outlook151
  • References152
  • Chapter 3. Structure, Function, and Biosynthesis of the Metallosulfur Clusters in Nitrogenases159
  • I. Introduction160
  • II. The Fe Proteins of Molybdenum Nitrogenase162
  • III. The MoFe Proteins166
  • IV. Biosynthesis of Molybdenum Nitrogenase174
  • V. The Mechanism of Molybdenum Nitrogenase183
  • VI. The Alternative Nitrogenases202
  • VII. Conclusions and Outlook211
  • References212
  • Chapter 4. The Search for a ''Prismane'' Fe–S Protein219
  • I. Introduction219
  • II. Historical Discovery of ''Prismane'' Protein (Now Termed Feps)221
  • III. Crystallographic Studies232
  • IV. Conclusion and Future Studies245
  • References247
  • Chapter 5. NMR Spectra of Iron–Sulfur Proteins251
  • I. Introduction251
  • II. Electron Relaxation Times252
  • III. Valence Delocalization257
  • IV. Considerations on the Reduction Potential265
  • V. Solution Structure266
  • VI. Folding271
  • VII. Perspectives276
  • References277
  • Chapter 6. Nickel–Iron–Sulfur Active Sites: Hydrogenase and CO Dehydrogenase283
  • I. Introduction283
  • II. General Concepts Regarding Nickel and Iron–Sulfur285
  • III. Hydrogenase286
  • IV. CODH/ACS305
  • V. Conclusions326
  • References327
  • Chapter 7. FeS Centers Involved in Photosynthetic Light Reactions335
  • I. Introduction335
  • II. 2[4Fe–4S] Proteins338
  • III. The Bridging Cluster FX344
  • IV. [2Fe–2S] Ferredoxins344
  • V. High-Potential Iron–Sulfur Proteins345
  • VI. The Rieske Protein347
  • VII. Evolutionary Remarks355
  • References356
  • Chapter 8. Simple and Complex Iron–Sulfur Proteins in Sulfate Reducing Bacteria361
  • I. Introduction361
  • II. Rubredoxin and Desulforedoxin362
  • III. Desulfoferrodoxin366
  • IV. Rubrerythrin367
  • V. Ferredoxins370
  • VI. Fuscoredoxin (Novel Fe–S Cluster)378
  • VII. APS Reductase382
  • VIII. Pyruvate–Ferredoxin Oxidoreductase385
  • IX. Sulfite Reductase386
  • X. Hydrogenase388
  • XI. Molybdopterin-Containing Enzymes in SRB395
  • XII. Concluding Remarks406
  • References411
  • Chapter 9. Application of EPR spectroscopy to the Structural and Functional Study of Iron–Sulfur P421
  • I. Introduction421
  • II. EPR Characteristics and Relaxation Properties of the Centers423
  • III. Application of EPR to the Structural Study of Iron–Sulfur Proteins450
  • IV. Application of EPR to the Functional Study of Iron–Sulfur Centers474
  • V. Conclusion484
  • Appendix: Spin–Lattice Relaxation Processes486
  • References487
  • Index499
  • Contents of Previous Volumes511
Book details
  • Vendor Elsevier S & T
  • SKU 9780120236473
  • ISBN-13 9780080550800
  • Author Cammack, Richard
  • Category Science
  • Subject Inorganic

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Advances in Inorganic Chemistry presents timely and informative summaries of the current progress in a variety of subject areas within inorganic chemistry, ranging from bioinorganic to solid state. This acclaimed serial features reviews written by experts in the area and is an indispensable reference to advanced researchers. Each volume of Advances in Inorganic Chemistry contains an index, and each chapter is fully referenced.