STUDIES OF O2 ACTIVATION BY MOSSBAUER SPECTROSCOPY

这里提出的研究试图确定分子的电子结构 用穆斯堡尔谱和电子能谱研究某些含铁酶 顺磁共振。实验内容包括：1)进一步研究 乌头酸酶的簇结构和反应机理 柠檬酸循环。2)继续研究非政府组织的性质 双加氧酶的活性部位。这些酶通过氧气分解儿茶酚。 并在芳香族化合物的生物降解中起着重要作用 生物圈中的化合物。3)继续进行穆斯堡尔研究 细胞色素氧化酶，呼吸链的末端酶。这个 该酶的A3位，即氧还原的位置，将用 从牛心线粒体、嗜热嗜热菌和 亚硝酸单胞菌。4)还提出了对木质素降解的研究。 来自真菌P.chrysosporium的酶。

The research proposed here seeks to determine the electronic structures of some iron containing enzymes using Mossbauer spectroscopy and electron paramagnetic resonance. The experiments include: 1) Further studies of the cluster structures and reaction mechanism of aconitase, a key enzyme in the citric acid cycle. 2) Continuation of research into the nature of the active sites of dioxygenases. These enzymes cleave catechols by oxygen insertion and are of major importance in the biodegradation of aromatic compounds in the biosphere. 3) Continuation of Mossbauer studies of cytochrome oxidase, the terminal enzyme of the respiratory chain. The a3-site of the enzyme, the locus of oxygen reduction, will be studied with enzymes isolated from beef heart mitochondria, Thermus thermophilus and Nitrosomonas europeae. 4) It is also proposed to study a lignin-degrading enzyme from the fungus P. chrysosporium.