Bioinspired catalysis : metal-sulfur complexes / / edited by Wolfgang Weigand and Philippe Schollhammer ; contributors Ulf-Peter Apfel [and thirty three others]

• Record Nr.: UNINA9910817867803321
• Pubbl/distr/stampa: Weinheim, Germany : , : Wiley-VCH, , 2015; ©2015
• ISBN: 3-527-66418-1; 3-527-66416-5; 3-527-66419-X
• Descrizione fisica: 1 online resource (438 p.)
• Disciplina: 541.2242
• Soggetti: Metal complexes
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Description based upon print version of record.
• Nota di bibliografia: Includes bibliographical references at the end of each chapters and index.
• Nota di contenuto: Bioinspired Catalysis; Contents; List of Contributors; Preface; Part I Primordial Metal-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; 2.4.1 Redox Catalysis; 2.4.2 Nonredox Fe-S Cluster-Based Catalysis; 2.5 Fe-S Clusters and Oxidative Stress; 2.6 Regulation of Protein Expression by Fe-S Clusters; 2.6.1 Eukaryotic Iron Regulatory Protein 1 (IRP1); 2.6.1.1 IRP1 and Fe-S Cluster Biogenesis; 2.6.1.2 Reactive Oxygen Species and IRP1 Fe-S Cluster Stability; 2.6.1.3 X-Ray Structural Studies of IRP1-IRE Complexes; 2.6.2 Bacterial Fumarate Nitrate Reduction Regulator (FNR); 2.6.3 The ISC Assembly Machinery Regulator IscR; 2.7 ConclusionReferences; 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; 3.4.1 Amine [N2Ni(μ-S2)Fe] Complexes; 3.4.2 Phosphine [P2Ni(μ-S2)Fe] Complexes; 3.4.3 Thiolate [SxNi(μ-Sy)Fe] Complexes; 3.4.4 Polymetallic [Ni(μ-S)zFey] Complexes; 3.5 Analogs of [NiFe] Hydrogenase Incorporating Proton Relays; 3.5.1 Nickel Complexes Incorporating Protonation Sites; 3.5.2 [NiFe] Complexes Incorporating Protonation Sites3.6 Perspectives and Future Challenges; Acknowledgments; 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; 4.3.1 Biomimetic Models of the ""Rotated State""; 4.3.2 Electron Transfer in [FeFe] Hydrogenase Models; 4.3.3 Protonation Chemistry of [FeFe] Hydrogenase Models; 4.3.3.1 Hydride Formation; 4.3.3.2 Ligand Protonation and Proton Relays; 4.3.4 Water-Soluble Hydrogenase Mimics; 4.4 Conclusion; References; Chapter 5 The Third Hydrogenase5.1 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; 5.6.1 Studies Before the Most Recent Assignment of the FeGP Cofactor; 5.6.2 Studies After the Most Recent Assignment of the FeGP Cofactor; 5.6.3 Synthesized Model Complexes of the FeGP Cofactor; References; Chapter 6 DFT Investigation of Models Related to the Active Site of Hydrogenases; 6.1 Introduction; 6.2 QM Studies of Hydrogenases
• Sommario/riassunto: 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.