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PublicationJournal of Biological Inorganic Chemistry
Year2008
Volume13
Pages1315-1320
International

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

Authors:Antonio López de Lacey, María Cristina Gutiérrez Sánchez, Víctor Manuel Fernández López, Isabel Pacheco Pérez, Ines A. C. Pereira
Groups of research:BioElectroCatalysis
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.
Keywords:Hydrogenase, Infrared, Selenocysteine, Spectroelectrochemistry
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