LEADER 05033nam 2200661 450 001 9910817867803321 005 20200520144314.0 010 $a3-527-66418-1 010 $a3-527-66416-5 010 $a3-527-66419-X 035 $a(CKB)3710000000222911 035 $a(EBL)1767040 035 $a(SSID)ssj0001400180 035 $a(PQKBManifestationID)11833582 035 $a(PQKBTitleCode)TC0001400180 035 $a(PQKBWorkID)11459040 035 $a(PQKB)11671108 035 $a(OCoLC)891398199 035 $a(MiAaPQ)EBC1767040 035 $a(Au-PeEL)EBL1767040 035 $a(CaPaEBR)ebr10909194 035 $a(CaONFJC)MIL637256 035 $a(OCoLC)888352800 035 $a(PPN)184618444 035 $a(EXLCZ)993710000000222911 100 $a20140901h20152015 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aBioinspired catalysis $emetal-sulfur complexes /$fedited by Wolfgang Weigand and Philippe Schollhammer ; contributors Ulf-Peter Apfel [and thirty three others] 210 1$aWeinheim, Germany :$cWiley-VCH,$d2015. 210 4$dİ2015 215 $a1 online resource (438 p.) 300 $aDescription based upon print version of record. 311 $a3-527-33308-8 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aBioinspired 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 327 $a2.2 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 327 $a2.7 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(?-S2)Fe] Complexes; 3.4.2 Phosphine [P2Ni(?-S2)Fe] Complexes; 3.4.3 Thiolate [SxNi(?-Sy)Fe] Complexes; 3.4.4 Polymetallic [Ni(?-S)zFey] Complexes; 3.5 Analogs of [NiFe] Hydrogenase Incorporating Proton Relays; 3.5.1 Nickel Complexes Incorporating Protonation Sites 327 $a3.5.2 [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 327 $aChapter 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 327 $a6.2 QM Studies of Hydrogenases 330 $aThis 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. 606 $aMetal complexes 615 0$aMetal complexes. 676 $a541.2242 702 $aWeigand$b Wolfgang 702 $aSchollhammer$b Philippe 702 $aApfel$b Ulf-Peter 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910817867803321 996 $aBioinspired catalysis$93965014 997 $aUNINA