Reactivity of [Fe] and [Ni-Fe-Se] hydrogenases with their oxido-reduction partner: the tetraheme cytochrome c3.
In order to understand the electron transfer mechanisms for the [Fe] and [Ni-Fe] hydrogenases, a kinetic study of cytochrome c3 reduction has been undertaken. Cyclic voltammetry and controlled-potential amperometry techniques have been used to investigate the intermolecular electron-transfer reaction between cytochrome c3 and [Fe] hydrogenase from Desulfovibrio vulgaris Hildenborough. Electron-transfer cross-reactions between [Fe] or [Ni-Fe-Se] hydrogenase and cytochrome c3 from Desulfovibrio vulgaris Hildenborough or Desulfovibrio desulfuricans Norway have been studied. Some structural implications are considered from these experimental data.
Bianco
P
P
Laboratoire de Chimie et Electrochimie des Complexes, C.N.R.S., Université de Provence, Marseille, France.
Haladjian
J
J
Bruschi
M
M
Guerlesquin
F
F
D003574:Cytochrome c Group / Q000378:metabolism*; D003901:Desulfovibrio / Q000378:metabolism*; D016969:Desulfovibrio vulgaris / Q000378:metabolism; D004563:Electrochemistry / Q000379:methods; D004579:Electron Transport; D006864:Hydrogenase / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D009532:Nickel / Q000378:metabolism*; D010084:Oxidation-Reduction; D012643:Selenium / Q000378:metabolism*
D003574:Cytochrome c Group; D009532:Nickel; C017165:cytochrome c(3); D007501:Iron; D006864:Hydrogenase; D012643:Selenium