期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1827, 期 8-9, 页码 986-1002出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2013.01.015
关键词
Oxygen-tolerant; Hydrogen; Spectroscopy; Electrochemistry; Renewable energy
资金
- Max Planck Society
- Alexander von Humboldt Foundation
Hydrogenase proteins catalyze the reversible conversion of molecular hydrogen to protons and electrons. The most abundant hydrogenases contain a [NiFe] active site; these proteins are generally biased towards hydrogen oxidation activity and are reversibly inhibited by oxygen. However, there are [NiFe] hydrogenase that exhibit unique properties, including aerobic hydrogen oxidation and preferential hydrogen production activity; these proteins are highly relevant in the context of biotechnological devices. This review describes four classes of these nonstandard [NiFe] hydrogenases and discusses the electrochemical, spectroscopic, and structural studies that have been used to understand the mechanisms behind this exceptional behavior. A revised classification protocol is suggested in the conclusions, particularly with respect to the term oxygen-tolerance. This article is part of a special issue entitled: metals in bioenergetics and biomimetics systems. (C) 2013 Elsevier B.V. All rights reserved.
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