MECHANISMS OF REACTIONS OF OXYGEN WITH HEME PROTEINS

详细研究了分子氧、碳 一氧化物、异氰化物、一氧化氮和氮氧碱转化为血红素 将制备蛋白质模型化合物。 将特别注意 这些系统中的皮秒动力学。 这些研究将提供 铁（II）卟啉的基本结合过程的机制， 缺乏蛋白质。 通过这种方式，可以分离蛋白质的影响 从基本的化学效应的动态过程中发生的， 氧气运输 第二，这些系统提供了新的方法， 研究更广泛意义的溶剂-双生对动力学的细节。 为了完成对孪生过程的研究， 自由基笼前体如卟啉金属-烷基的光解 配合物和烯酮亚胺，R2 C =C=N-R'也将被检查。 为了了解一氧化氮相互作用的生物学效应，详细 模型血红素-NO的平衡和秒至皮秒动力学研究 将研究复合物。 NO的结构和环境效应 结合动力学和平衡，并对血红素-NO的形成， 将详细研究碱性血红素-NO。 pH对NO结合的影响， 近基解离和皮秒NO动力学将研究与 肌红蛋白和其他血红素蛋白。 新的模型系统设计来模拟蛋白质蛔虫血红蛋白和 将制备具有高极性口袋的过氧化物酶。 这些模型 将提供当前讨论中所需的基本结构效应， 极性对蛋白质行为的影响。

Detailed studies of structure-reactivity in the binding of dioxygen, carbon monoxide, isocyanides, nitric oxide and nitrogen and oxygen bases to heme protein model compounds will be made. Special attention will be given to the picosecond kinetics in these systems. These studies will provide the mechanisms of the fundamental binding processes with iron(II) porphyrins in the absence of proteins. In this way the protein effects can be separated from the basic chemical effects in the dynamic processes occurring in oxygen transport. Secondly, these systems provide new approaches to the study of details of solvent-geminate pair dynamics of broader significance. To complete the study of geminate processes the picosecond relaxation after photolysis of free radical cage precursors such as porphyrin metal-alkyl complexes and ketenimines, R2C=C=N-R' will also be examined. To understand the biological effects of nitric oxide interactions, detailed equilibrium and second to picosecond kinetic studies of model heme-NO complexes will be studied. Structural and environmental effects on NO binding kinetics and equilibria and on the formation of Heme-NO from Base-Heme-NO will be studied in detail. The effect of pH on NO binding, proximal base dissociation and picosecond NO kinetics will be studied with myoglobin and other heme proteins. New model systems designed to mimic the proteins ascaris hemoglobin and peroxidases which have highly polar pockets will be prepared. These models will provide basic structural effects needed in the current discussions of the effects of polarity in protein behavior.