FTIR spectroelectrochemical characterization of the Ni-Fe-Se hydrogenase from Desulfovibrio vulgaris Hildenborough.
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.
De Lacey
Antonio L
AL
Instituto de Catálisis y Petroleoquímica, CSIC, C/Marie Curie 2, 28049, Madrid, Spain. alopez@icp.csic.es
Gutiérrez-Sánchez
Cristina
C
Fernández
Víctor M
VM
Pacheco
Isabel
I
Pereira
Inês A C
IA
D002384:Catalysis; D020134:Catalytic Domain; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D004563:Electrochemistry; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D006864:Hydrogenase / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D017550:Spectroscopy, Fourier Transform Infrared
C058560:nickel-iron-selenium hydrogenase; D006864:Hydrogenase