Bioinspired catalysis : metal-sulfur complexes /: metal-sulfur complexes. (2015)

• Record Type: Book
• Further Information: Note: Edited by Wolfgang Weigand and Philippe Schollhammer ; contributors Ulf-Peter Apfel [and thirty three others].
• Editors: Weigand, Wolfgang; Schollhammer, Philippe
• Other Names: Apfel, Ulf-Peter contributor.
• Contents: 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.
• Publisher Details: Weinheim, Germany : Wiley-VCH
• Publication Date: 2015
• Copyright Date: 2015
• Extent: 1 online resource (438 pages), illustrations
• Subjects: 541.2242; Metal complexes; SCIENCE -- Chemistry -- Inorganic; Metal complexes; Electronic books
• Languages: English
• ISBNs: 9783527664160; 3527664165; 9783527664191; 9783527664184; 3527664181; 9783527664177; 3527664173; 3527333088; 9783527333080
• Related ISBNs: 352766419X; 9783527333080
• Notes: Note: Includes bibliographical references at the end of each chapters and index.; Note: Online resource; title from PDF title page (ebrary, viewed August 30, 2014).
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.