The sulfate-reducing bacterium Desulfovibrio vulgaris Miyazaki F contains multiple types of hydrogenase proteins; in selenium-enriched environments, a [NiFe] hydrogenase containing a terminal selenocysteine ligand to the nickel center is preferentially expressed.  This protein exhibits unique behavior with respect to catalysis and deactivation mechanisms than the standard [NiFe] hydrogenase.  We report the isolation and characterization of a membrane-bound [NiFeSe] hydrogenase and present electrochemical results that indicate H2 production activity that persists in the presence of oxygen.  EPR and infrared spectroscopic characterization reveal differences in the electronic structure of the active site; these features will be discussed in the context of enzymatic differences between the standard [NiFe] and the [NiFeSe] hydrogenases.

Spectroscopic and electrochemical investigations of a new [NiFeSe] hydrogenase

244th National Meeting (2012)

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