CO dehydrogenase from Clostridium thermoaceticum. EPR and electrochemical studies in CO2 and argon atmospheres.
The EPR and redox properties of the metal complexes in CO dehydrogenase (CODH) from Clostridium thermoaceticum were studied. Controlled potential coulometric reductive titrations of CODH were performed under argon and CO2 atmospheres. In the titrations performed under argon, five to eight electrons/dimer were required for reduction, and four distinct EPR signals appeared. These included a signal with gave = 1.82 (Em approximately -220 mV), two signals with the same g values but different linewidths at gave = 1.94 (Em approximately -440 mV), and a signal at gave = 1.86 (Em approximately -530 mV). All of the S = 1/2 EPR signals had low spin concentrations; values between 0.2 and 0.3 spins/dimer were typically obtained for each signal. Features between g = 6 and 4, typical of S = 3/2 states, were also observed, and these may account, at least to some degree, for the low spin concentration values. Under CO2, and at negative potentials, CODH served as an electrocatalyst in the reduction of CO2 to CO. The apparent half-maximal activity for this reduction at pH 6.3 occurred at -430 mV, a potential near the thermodynamic value. An EPR signal, arising from a complex containing Ni, Fe, and the carbon from CO/CO2 developed along with this activity. The reduction of this complex is probably the last step to occur prior to the catalysis of CO2 reduction.
Lindahl
P A
PA
Gray Freshwater Biological Institute, University of Minnesota, Navarre 55392.
Münck
E
E
Ragsdale
S W
SW
D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D001128:Argon / Q000494:pharmacology*; D002245:Carbon Dioxide / Q000494:pharmacology*; D003013:Clostridium / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D007700:Kinetics; D009097:Multienzyme Complexes; D010084:Oxidation-Reduction; D011199:Potentiometry
D009097:Multienzyme Complexes; D002245:Carbon Dioxide; D001128:Argon; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase