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Title: /sup 13/C and /sup 61/Ni isotope substitutions confirm the presence of a nickel(III)-carbon species in acetogenic CO dehydrogenases

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)

The nickel-containing CO dehydrogenase from Acetobacterium woodii and Clostridium thermoaceticum were studied by EPR spectroscopy in order to define the components involved in the EPR spectrum obtained by reaction of the enzymes with the substrate, CO. Using isotopic substitution techniques, these experiments unequivocally establish that a nickel-carbon species is involved in the g=2.08, 2.02 EPR signal. Comparing the /sup 61/Ni- and /sup 59/Ni-substituted enzymes, the g=2.08 component of the resonance was found to be mainly due to nickel with a smaller contribution by the carbon species. Reaction of the CO dehydrogenase with (/sup 13/C)CO versus (/sup 12/C)CO showed that a carbon species, formed from CO, was the major contributor to the g=2.02 EPR signal. In addition, the oxidized CO dehydrogenase was found to exhibit a Ni(III) EPR signal analogous to that of the hydrogenase from the methanogenic and sulfate-reducing bacteria. 19 references, 3 figures.

Research Organization:
Univ. of Georgia, Athens
DOE Contract Number:
AS09-79ER10499
OSTI ID:
5960072
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Vol. 115:2
Country of Publication:
United States
Language:
English

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