RESONANCE SPECTROSCOPY OF METALLOPROTEINS

拟议研究的目的是阐明电子结构。 主要使用穆斯堡尔、EPR和Endor的金属蛋白质活性中心的研究 光谱学。特别令人感兴趣的是相互作用的血红素蛋白。 与O2或H_2O_2及其各种中间体反应。最终目标是 了解控制反应性和稳定性的结构和动态特征 功能。将研究以下系统：(I)正在进行的工作 细菌单加氧酶中O2的活化和产物的形成 细胞色素P450cam将继续。早些时候的数据表明，一个电子 可转移到细胞色素P450与cam的三元络合物 通过低温X射线照射衬底和O2，以及新EPR- 在逐步退火到更高的温度下，形成了活性血红素物种 温度。我们将探索这些中间体的性质，并 将对反应产物进行分析。低温技术将 也可用于在产品形成步骤中搜索中间体 天然系统和改良的底物和蛋白质。(Ii)李国能教授。 斯利格的团队已经生产出转基因肌红蛋白，这将是 由穆斯堡尔、EPR和Endor光谱在合作中表征 努力将氨基酸替换与功能变化联系起来， 结构和电子态。(Iii)木质素和木质素的穆斯堡尔研究 白腐菌黄孢原毛平革菌的锰过氧化物酶 以及它们与过氧化氢和底物的反应产物将在 与俄勒冈州研究生院戈尔德教授合作。(四)两个 来自大肠杆菌的末端氧化酶，细胞色素o和细胞色素d，将是 由EPR、Endor和穆斯堡尔谱学与 甘尼斯教授。(5)关于杂氰菊酯和结构上相关的双核的工作 铁蛋白和模型化合物将继续存在。

The aim of the proposed research is to elucidate the electronic structures of metallo-protein active centers using primarily Mossbauer, EPR, and ENDOR spectroscopy. Of particular interest are the heme proteins that interact with O2 or H2O2 and their various intermediates. The ultimate goal is to understand the structural and dynamic features that control reactivity and function. The following systems will be studied: (i) Work in progress on O2 activation and product formation in the bacterial monoxygenase cytochrome P450cam will continue. Earlier data suggest that an electron can be transferred to the ternary complex of cytochrome P450cam with substrate and O2 by low-temperature X-ray irradiation, and that new EPR- active heme species are formed on stepwise annealing to higher temperatures. The nature of these intermediates will be explored and the products of the reaction will be analyzed. Low-temperature techniques will also be used to search for intermediates in the product-forming steps of the native system and with modified substrates and proteins. (ii) Prof. Sligar's group has produced genetically modified myoglobins, which will be characterized by Mossbauer, EPR and ENDOR spectroscopy in a collaborative effort to correlate amino acid substitutions with changes in function, structure and electronic state. (iii) A Mossbauer study of lignin and manganese peroxidase from the white rot fungus Phanerochaete chrysosporium and of their reaction products with H2O2 and substrate will be started in collaboration with Prof. Gold, Oregon Graduate Institute. (iv) Two terminal oxidases, cytochrome o and cytochrome d from E. coli, will be investigated by EPR, ENDOR and Mossbauer spectroscopy in collaboration with Prof. Gennis. (v) Work on hemerythrin and structurally related binuclear iron proteins and model compounds will continue.