NiFe] hydrogenases: a common active site for hydrogen metabolism under diverse conditions.

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. Copyright © 2013 Elsevier B.V. All rights reserved.

Citation

Hannah S Shafaat, Olaf Rüdiger, Hideaki Ogata, Wolfgang Lubitz. NiFe] hydrogenases: a common active site for hydrogen metabolism under diverse conditions. Biochimica et biophysica acta. 2013 Aug-Sep;1827(8-9):986-1002

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PMID: 23399489

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