Bioinspired catalysis : metal-sulfur complexes

Bioinspired catalysis : metal-sulfur complexes
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仿生催化:金属硫络合物

DOI:
10.1002/9783527664160
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发表时间:
2014
期刊:
影响因子:
2.8
通讯作者:
P. Schollhammer
P. Schollhammer
中科院分区:
化学2区
文献类型:
--
作者:
Wolfgang Weigand;P. Schollhammer

文献摘要

被引文献

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第一部分:初级金属-硫介导的反应从化学不变性到遗传变异性Fe-S簇:生物发生和氧化还原,催化和调节性质第二部分:氢化酶活性位点的模型复合物-质子和双氢活化[NiFe]氢化酶[Fe-Fe]氢化酶模型:氢化酶第三代DFT研究综述氢化酶活性中心相关模型生物放氢机理研究第三部分:固氮酶活性中心的结构与功能固氮酶活性中心模型复合物的研究进展固氮酶结合底物催化合成Fe-S簇合物氢化反应的统一化学机理及其与固氮酶的关系第四部分:杂项RCN活化、DMSO还原腈水合酶的硫-氧化和功能模型钼和钨氧化还原酶模型第V部分:电极材料与人工光合系统的应用前景
PART I: PRIMORDIAL METAL-SULFUR MEDIATED REACTIONS From Chemical Invariance to Genetic Variability Fe-S Clusters: Biogenesis and Redox, Catalytic and Regulatory Properties PART II: MODEL COMPLEXES OF THE ACTIVE SITE OF HYDROGENASES - PROTON AND DIHYDROGEN ACTIVATION [NiFe] Hydrogenases [Fe-Fe]Hydrogenases Models: An Overview The Third Hydrogenase DFT Investigation of Models Related to the Active Site of Hydrogenases Mechanistic Aspects of Biological Hydrogen Evolution and Uptake PART III: NITROGEN FIXATION Structures and Functions of the Active Site of Nitrogenases Model Complexes of the Active Site of Nitrogenases: Recent Advances A Unified Chemical Mechanism for Hydrogenation Reactions Catalysed by Nitrogenase Binding Substrates to Synthetic Fe-S-Based Clusters and the Possible Relevance to Nitrogenases PART IV: MISCELLANEOUS: RCN ACTIVATION, DMSO REDUCTION Sulfur-Oxygenation and Functional Models of Nitrile Hydratase Molybdenum and Tungsten Oxidoreductase Models PART V: APPLICATIVE PERSPECITVES Electrode Materials and Artificial Photosynthetic Systems