FTIR spectroelectrochemical characterization of the Ni–Fe–Se hydrogenase from Desulfovibrio vulgaris Hildenborough |
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Authors: | Antonio L De Lacey Cristina Gutiérrez-Sánchez Víctor M Fernández Isabel Pacheco Inês A C Pereira |
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Institution: | (1) Instituto de Catálisis y Petroleoquímica, CSIC, C/Marie Curie 2, 28049 Madrid, Spain;(2) Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal |
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Abstract: | 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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Keywords: | Hydrogenase Infrared Selenocysteine Spectroelectrochemistry |
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