JBIC Journal of Biological Inorganic Chemistry

, Volume 13, Issue 8, pp 1315–1320

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
Original Paper

DOI: 10.1007/s00775-008-0412-5

Cite this article as:
De Lacey, A.L., Gutiérrez-Sánchez, C., Fernández, V.M. et al. J Biol Inorg Chem (2008) 13: 1315. doi:10.1007/s00775-008-0412-5

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.

Keywords

Hydrogenase Infrared Selenocysteine Spectroelectrochemistry 

Copyright information

© SBIC 2008

Authors and Affiliations

  • Antonio L. De Lacey
    • 1
  • Cristina Gutiérrez-Sánchez
    • 1
  • Víctor M. Fernández
    • 1
  • Isabel Pacheco
    • 2
  • Inês A. C. Pereira
    • 2
  1. 1.Instituto de Catálisis y Petroleoquímica, CSICMadridSpain
  2. 2.Instituto de Tecnologia Química e BiológicaUniversidade Nova de LisboaOeirasPortugal

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