X-ray structural study of the membrane-bound[NiFe]-hydrogenase

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Hydrogenases play key roles in hydrogen metabolism by catalyzing synthesis and decomposition of molecular hydrogen. While most of the hydrogenases exhibit no activity in the presence of O2, the membrane-bound[NiFe]-hydrogenase is known to be O2-tolerant, of which mechanism had been poorly understood. In this study, X-ray crystal structures of the membrane-bound[NiFe]-hydrogenase have been determined for three different redox states at resolutions of 1.2-1.4 A. One of the Fe-S clusters showed an unprecedented structure and its redox dependent conformational changes, to which the O2-tolerant property of this hydrogenase should be ascribable.