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Bioinspired Catalysis : Metal-Sulfur Complexes /
This book provides an overview of bioinspired metal-sulfur catalysis by covering structures, activities and model complexes of enzymes exhibiting metal sulphur moieties in their active center.
| Clasificación: | Libro Electrónico |
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| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Weinheim :
Wiley-VCH,
2014.
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| Temas: | |
| Acceso en línea: | Texto completo |
Tabla de Contenidos:
- Related Titles; Title Page; Copyright; List of Contributors; Preface; Part I: PrimordialMetal-Sulfur-Mediated Reactions; Chapter 1: From Chemical Invariance to Genetic Variability; 1.1 Heuristic of Biochemical Retrodiction; 1.2 Retrodicting the Elements of Life; 1.3 Retrodicting Pioneer Catalysis; 1.4 Retrodicting Metabolic Reproduction and Evolution; 1.5 Retrodicting Pioneer-Metabolic Reactions; 1.6 Early Evolution in a Spatiotemporal Flow Context; Acknowledgments; References; Chapter 2: Fe-S Clusters: Biogenesis and Redox, Catalytic, and Regulatory Properties; 2.1 Introduction.
- 2.2 Fe-S Cluster Biogenesis and Trafficking2.3 Redox Properties of Fe-S Clusters; 2.4 Fe-S Clusters and Catalysis; 2.5 Fe-S Clusters and Oxidative Stress; 2.6 Regulation of Protein Expression by Fe-S Clusters; 2.7 Conclusion; References; Part II: Model Complexes of the Active Site of Hydrogenases
- Proton and Dihydrogen Activation; Chapter 3: [NiFe] Hydrogenases; 3.1 Introduction; 3.2 Introduction to [NiFe] Hydrogenases; 3.3 Nickel Thiolate Complexes as Analogs of [NiFe] Hydrogenase; 3.4 [NiFe] Hydrogenase Model Complexes; 3.5 Analogs of [NiFe] Hydrogenase Incorporating Proton Relays.
- 3.6 Perspectives and Future ChallengesAcknowledgments; References; Chapter 4: [FeFe] Hydrogenase Models: an Overview; 4.1 Introduction; 4.2 Synthetic Strategies toward [FeFe] Hydrogenase Model Complexes; 4.3 Properties of Model Complexes; 4.4 Conclusion; References; Chapter 5: The Third Hydrogenase; 5.1 Introduction; 5.2 Initial Studies of Hmd; 5.3 Discovery that Hmd Contains a Bound Cofactor; 5.4 Discovery that Hmd is a Metalloenzyme; 5.5 Crystal Structure Studies of [Fe] Hydrogenase; 5.6 Mechanistic Models of [Fe] Hydrogenase; References.
- Chapter 6: DFT Investigation of Models Related to the Active Site of Hydrogenases6.1 Introduction; 6.2 QM Studies of Hydrogenases; 6.3 QM Studies of Synthetic Complexes Related to the Active Site of Hydrogenases; 6.4 Conclusions; References; Chapter 7: Mechanistic Aspects of Biological Hydrogen Evolution and Uptake; 7.1 Introduction; 7.2 [FeFe] Hydrogenases; 7.3 [NiFe] Hydrogenases; 7.4 [Fe] Hydrogenase; 7.5 Nitrogenase; References; Part III: Nitrogen Fixation; Chapter 8: Structures and Functions of the Active Sites of Nitrogenases; 8.1 Introduction; 8.2 Properties of Mo Nitrogenase.
- 8.3 Catalysis by Mo Nitrogenase8.4 Unique Features of V Nitrogenase; 8.5 Catalytic Properties of Isolated FeMo-co and FeVco; Acknowledgments; References; Chapter 9: Model Complexes of the Active Site of Nitrogenases: Recent Advances; 9.1 Introduction; 9.2 Structural Models of Metal-Sulfur Clusters in the Nitrogenases; 9.3 Functional Modeling at a Single Molybdenum Center; 9.4 Functional Modeling at a Single Iron Center; 9.5 The Hydrogen and Homocitrate Issues in Nitrogenase Model Chemistry; 9.6 Sulfur- and Metal-Metal Interaction in Functional Models of Nitrogenase.