Hydrogenases are enzymes nature uses to catalyze the activationof hydrogen. These enzymes are being studied with the goal of developing bothphotobiological and photohybrid hydrogen production systems.  Hydrogenases are also inspiring novelbiomimetic catalysts for replacing expensive platinum and palladium basedcatalysts.  The catalytic site of the[FeFe]-hydrogenases contains the H-cluster, a [6Fe-6S]-cluster composed of aconventional [4Fe-4S]-cluster coordinated to a unique [2Fe-2S]-cluster withcarbon monoxide and cyanide ligation. Infrared spectroscopy is a useful techniqueto characterize the CO and CN ligands, and elucidate structural changes to theH-cluster associated with various redox active states of the enzyme. Thistechnique also allows comparison of different hydrogenases and studyingthe effect protein structure has on the H-cluster, measured by changes inthe IR spectrum. Two different hydrogenases were characterized, and preliminarydevelopment of a surface sensitive technique is designed to characterize theseenzymes on surfaces under various conditions.

Applications of infrared spectroscopy to the characterization of [FeFe]-hydrogenases

242nd National Meeting (2011)

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