RAMAN STUDIES OF SULFITE REDUCTASES AND OTHER ENZYMES

我们建议研究蛋白质环境和/或发色团 相互作用控制了一种 使用共振拉曼光谱法， 不同亚硫酸盐还原酶中siroheme和铁硫簇 硫酸盐还原菌。 共振拉曼光谱 可以产生发色团的详细分子信息， 无法通过其他方法获得。 亚硫酸盐还原酶催化 亚硫酸盐到硫化物的六电子还原。 所述降低是 对含硫细胞成分的合成和 硫酸盐还原菌的终末呼吸。 虽然 亚硫酸盐还原酶含有相同的两个发色团， 性质是完全不同的，使它们成为理想的系统， 研究反应性的结构变化。 为了 了解发色团的拉曼光谱，我们计划 研究各种溶液中的发色团及其类似物， 环境. 我们还建议研究亚硫酸盐的作用机理 还原酶的变化，通过检查发色团在 催化，在不同的氧化还原电位，并结合到不同的 印刷受体. 我们还建议表征其他铁的发色团- 来自硫酸盐还原菌的硫蛋白。

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.