期刊
CHEMICAL SOCIETY REVIEWS
卷 50, 期 3, 页码 1668-1784出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0cs01089h
关键词
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资金
- Deutsche Forschungsgemeinschaft [AP242/2-1, AP242/12-1, EXC 2033 - 390677874]
- Fraunhofer Internal Programs [Attract 097-602175]
- German Academic Exchange Service DAAD
- Studienstiftung des Deutschen Volkes
This review provides an overview of developments in [FeFe]-hydrogenase research, focusing on synthetic mimics and their application within the native enzymatic environment.
While hydrogen plays an ever-increasing role in modern society, nature has utilized hydrogen since a very long time as an energy carrier and storage molecule. Among the enzymatic systems that metabolise hydrogen, [FeFe]-hydrogenases are one of the most powerful systems to perform this conversion. In this light, we will herein present an overview on developments in [FeFe]-hydrogenase research with a strong focus on synthetic mimics and their application within the native enzymatic environment. This review spans from the biological assembly of the natural enzyme and the highly controversial discussed mechanism for the hydrogen generation to the synthesis of multiple mimic platforms as well as their electrochemical behaviour.
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