The F430 Cofactor of S-Methyl Coenzyme M Reductase

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Chemical, biochemical and biophysical investigations of the nickel containing cofactor, F430. will be pursued. This cofactor is a required component of the enzyme methyl reductase, obtained form the methanogenic archaebacteria Methanobacterium thermoautotrophicum, which catalyzes the reductive conversion of a sulfur-bonded methyl group to methane. Dr. Scott is interested in the involvement or role of the nickel in the production of the methane. he will first investigate the coordination chemistry of the nickel containing cofactor both in the isolated and in the enzyme-bond state. He will use a number of spectroscopic techniques (UV-visible, resonance Raman, magnetic circular dichroism, and nuclear magnetic resonance) to identify the ligands to the nickel of the cofactor in the purified enzyme. he will try to generate, isolate and characterize the lower oxidation state nickel forms of (1) the enzyme in intact cells, (2) the enzyme in purified form and (3) the cofactor alone to test the hypothesis that the lower oxidation state nickel form is the actual form obtaining in vivo.