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

Antonio L. De Lacey, Cristina Gutiérrez-Sánchez, Víctor M. Fernández, Isabel Pacheco, Inês A.C. Pereira

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29 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1315-1320
Number of pages6
JournalJournal of Biological Inorganic Chemistry
Volume13
Issue number8
DOIs
Publication statusPublished - 1 Nov 2008

Keywords

  • Hydrogenase
  • Infrared
  • Selenocysteine
  • Spectroelectrochemistry

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