ChemInform Abstract: X‐Ray Absorption Spectroscopic Evidence for a Unique Nickel Site in Clostridium thermoaceticum Carbon Monoxide Dehydrogenase

Abstract

Carbon monoxide dehydrogenase (COdH) in Clostridium thermoaceticum is an ..cap alpha../sub 3/..beta../sub 3/ protein containing six nickels per molecule, in addition to a number of Fe-S clusters. Previous electron paramagnetic resonance (EPR) spectroscopic work has suggested that nickel is involved in binding CO forming an EPR-detectable species, which is probably a key intermediate in the oxidation of CO to CO/sub 2/ and in the synthesis of acetate. In order to better define the nature of this nickel site, Ni X-ray absorption spectra have been recorded and interpreted by comparison with model compounds. The extended X-ray absorption fine structure (EXAFS) spectrum for oxidized COdH is different from that of other Ni enzymes. Both the EXAFS and the X-ray absorption edge spectra suggest a Ni site containing substantial sulfur ligation. The Ni X-ray absorption edge spectrum of rubredoxin-oxidized COdH exhibits a characteristic shoulder with an inflection point at 8336 eV. Such a feature is absent in octahedral model compounds, whereas a well-resolved peak is observed in square-planar Ni complexes. A distinct 1s ..-->.. 3d transition at 8333 eV is observed in a tetrahedral model. The lack of correspondence suggests that square-pyramidal and distorted-square-planar geometries are plausible candidates for the COdH Ni site.more » Treatment of rubredoxin-oxidized COdH with hydrogenase and H/sub 2/ shifts the Ni edge to lower energies, indicating Ni-based reduction. 34 references, 3 figures.« less