MOSSBAUER STUDIES OF IRON-CONTAINING PROTEINS & ENZYMES

穆斯堡尔谱的研究主要针对以下酶：（1）氢化酶 来自巴氏梭菌W5和来自硫酸盐还原菌，（2） 来自硫杆菌的氮化物还原酶，和（3）亚硫酸盐 T.细菌和硫酸盐还原菌。 氢化酶能够激活分子氢和许多 微生物用它来代谢氢气。 了解氢化酶 机制可能是催化制氢的关键一步， 水和太阳能，一种潜在的重要替代能源。 亚硝酸盐还原酶将亚硝酸盐还原为一氧化氮，而亚硫酸盐还原酶 催化亚硫酸盐到硫化物的6电子还原。 这些减少 亚硝酸盐和亚硫酸盐，分别是硝酸盐和亚硫酸盐的基本步骤， 硫酸盐呼吸 尽管这些酶的生物学重要性 功能，其假体组知之甚少。 拟议 研究应该揭示物理性质和结构信息 与这些酶的辅基有关;基本信息 了解各自的机制。 结果将 与EPR，NMR，ENDOR和光学数据相关，并希望将 提供了一个健全的实验基础，详细的物理模型， 假体组。

Mossbauer studies are proposed for the following enzymes: (1) hydrogenases from Clostridium pasteurianum W5 and from sulfate-reducing bacteria, (2) nitride reductase from Thiobacillus denitrificans, and (3) sulfite reductases from T. denitrificans and sulfate-reducing bacteria. Hydrogenase is capable of activating molecular hydrogen and many micro-organisms use it to metabolize H2. Understanding the hydrogenase mechanism could be a key step toward catalysis of hydrogen production from water and solar energy, a potentially important alternate energy source. Nitrite reductase reduces nitrite to nitric oxide, while sulfite reductase catalyzes the 6-electron reduction of sulfite to sulfide. These reductions of nitrite and sulfite are, respectively, essential steps in nitrate and sulfate respirations. Despite the importance of these enzyme's biological functions, their prosthetic groups are poorly understood. The proposed studies should reveal physical properties and structural information pertinent to the prosthetic groups of these enzymes; information essential to the understanding of their respective mechanisms. The results will be correlated with EPR, NMR, ENDOR, and optical data, and hopefully will provide a sound experimental basis for detailed physical models of the prosthetic groups.