The F430 Cofactor of S-Methyl Coenzyme M Reductase

含镍辅因子F430的化学、生化和生物物理研究将会被追查。这种辅因子是甲基还原酶的必需成分，该酶是从产甲烷的古细菌甲烷自养杆菌获得的，它催化硫键甲基还原转化为甲烷。斯科特博士感兴趣的是镍在甲烷生产过程中的参与或作用。他将首先研究含镍辅因子在分离状态和酶键态下的配位化学。他将使用一些光谱技术(紫外可见、共振拉曼、磁圆二色谱和核磁共振)来鉴定纯化酶中辅因子镍的配体。他将尝试产生、分离和表征(1)完整细胞中的酶、(2)纯化形式的酶和(3)单独的辅因子的低氧化态镍形态，以检验低氧化态镍形态是在体内获得的实际形态的假设。

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.