A METHYLNICKEL INTERMEDIATE IN A BIMETALLIC MECHANISM OF ACETYL-COENZYME-A SYNTHESIS BY ANAEROBIC-BACTERIA

Resonance Raman (RR) spectroscopy was used to identify a methylnickel adduct (nu(Ni-C) = 422 wave numbers) of carbon monoxide dehydrogenase (CODH) from Clostridium thermoaceticum. Formed at a nickel/iron-sulfur cluster on CODH called center A, the methylnickel species is the prec ursor of the methyl group of acetyl-coenzyme A in an anaerobic pathway of carbon monoxide or carbon dioxide fixation. Rapid kinetic and RR s tudies demonstrated that methylation of nickel occurs by heterolysis o f the methyl-cobalt bond (nu(Co-C) = 429 wave numbers) of a methylated corrinoid/iron-sulfur protein. In combination with the earlier findin g of an iron-carbonyl adduct at center A, defection of the methylnicke l intermediate establishes a bimetallic mechanism for acetyl-coenzyme A synthesis.