The F430 Cofactor of S-Methyl Coenzyme M Reductase

化学、生物化学和生物物理研究 含镍辅因子，F430。将被追究。 这 辅因子是酶甲基化所必需的成分 还原酶，从产甲烷古细菌中获得 热自养甲烷杆菌，它催化 将硫键合的甲基还原转化为 甲烷 斯科特博士感兴趣的是参与或作用 在甲烷的生产过程中镍的含量。 他将首先 研究了含镍的配位化学 辅因子在分离和酶键状态。 他将使用一些光谱技术（紫外可见， 共振拉曼、磁性圆二色性和核 磁共振）来鉴定镍的配体， 纯化酶中的辅因子。 他将试图创造， 分离和表征较低氧化态镍形式 （1）完整细胞中的酶，（2）纯化的酶 形式和（3）单独的辅因子来检验假设， 较低氧化态的镍形式是获得的实际形式 in vivo.

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.