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J Biol Inorg Chem. 2008 Nov;13(8):1315-20. doi: 10.1007/s00775-008-0412-5. Epub 2008 Aug 13.

FTIR spectroelectrochemical characterization of the Ni-Fe-Se hydrogenase from Desulfovibrio vulgaris Hildenborough.

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  • 1Instituto de Catálisis y Petroleoquímica, CSIC, C/Marie Curie 2, 28049, Madrid, Spain.


For the first time a complete characterization by infrared spectroscopy of a Ni-Fe-Se hydrogenase in its different redox states is reported. The Ni-Fe-Se hydrogenase was isolated from Desulfovibrio vulgaris Hildenborough. Two different electron paramagnetic resonance silent and air-stable redox states that are not in equilibrium were detected. Upon reduction of these states the catalytically active states Ni-R and Ni-C appear immediately. These states are in redox equilibrium and their formal redox potential has been measured. Putative structural differences between the redox states of the active site of the Ni-Fe-Se hydrogenase are discussed.

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