title: [NiFe] hydrogenases: a common active site for hydrogen metabolism under diverse conditions.
abstract: 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.
authors: Max-Planck-Institut für Chemische Energiekonversion, Mülheim an der Ruhr, Germany.
authors: Hannah S
authors: HS
authors: Shafaat
authors: Olaf
authors: O
authors: Rüdiger
authors: Hideaki
authors: H
authors: Ogata
authors: Wolfgang
authors: W
authors: Lubitz
mesh_terms: D055162:Biocatalysis; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006859:Hydrogen / Q000378:metabolism*; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010084:Oxidation-Reduction
chemical_list: D006859:Hydrogen; C043296:nickel-iron hydrogenase; D006864:Hydrogenase
keywords: Electrochemistry; Hydrogen; Oxygen-tolerant; Renewable energy; Spectroscopy