| Literature DB >> 18704522 |
Antonio L De Lacey1, Cristina Gutiérrez-Sánchez, Víctor M Fernández, Isabel Pacheco, Inês A C Pereira.
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.Entities:
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Year: 2008 PMID: 18704522 DOI: 10.1007/s00775-008-0412-5
Source DB: PubMed Journal: J Biol Inorg Chem ISSN: 0949-8257 Impact factor: 3.358