RAMAN STUDIES OF SULFITE REDUCTASES AND OTHER ENZYMES

我们建议研究蛋白质环境和/或生色团 交互作用控制 利用共振拉曼光谱研究生色团 不同亚硫酸盐还原酶中的含铁血红素和铁硫团簇 来自硫酸盐还原细菌。共振拉曼光谱 可以获得发色团的详细分子信息 其他方法无法进行现场测试。亚硫酸盐还原酶催化 亚硫酸盐的6电子还原为硫化物。减价幅度为 对合成含硫细胞成分和In至关重要 硫酸盐还原细菌的终末呼吸作用。虽然 亚硫酸盐还原酶含有相同的两个发色团，它们的 属性非常不同，这使它们成为 研究具有反应性的结构变化。为了 了解发色团的拉曼光谱，我们计划 研究生色团及其在不同溶液中的类似物 环境。我们还建议研究亚硫酸盐的作用机理。 通过检测生色团的变化来还原酶 催化作用，在不同的氧化还原电位下，结合不同的 底物。 我们还建议对其他铁的生色团进行表征。 硫酸盐还原菌中的硫蛋白。

We propose to study how protein environment and/or chromophore interaction controls the properties and reactivity of a chromophore using resonance Raman spectroscopy by examining siroheme and iron-sulfur clusters in different sulfite reductases from sulfate reducing bacteria. Resonance Raman spectroscopy can yield detailed molecular information of the chromophore in situ unavailable by other methods. Sulfite reductases catalyze the 6-electron reduction of sulfite to sulfide. The reduction is crucial for synthesis of sulfur-containing cell constituents and in terminal respiration for sulfate reducing bacteria. Although sulfite reductases contain the same two chromophores, their properties are quite different, making them ideal systems for studying structural changes with reactivity. In order to understand the Raman spectra of the chromophores, we plan to study the chromophores and their analogs in various solutions and environments. We also propose to study the mechanism of sulfite reductases by examining changes in the chromophores during catalysis, at different redox potentials, and bound to different substrates. We also propose to characterize the chromophores of other iron- sulfur proteins from sulfate reducing bacteria.