MECHANISMS OF REACTIONS OF OXYGEN WITH HEME PROTEINS

氧、碳结合中结构-反应性的详细研究 一氧化碳、异氰化物、一氧化氮和氮氧碱生成亚铁血红素 将制作蛋白质模型化合物。我们将特别注意以下事项 这些系统中的皮秒动力学。这些研究将提供 铁(II)-卟啉的基本结合机理 蛋白质的缺失。通过这种方式，可以分离蛋白质的影响 从发生在动态过程中的基本化学效应 氧气输送。其次，这些系统提供了新的方法来 研究溶剂-双酯对动力学的细节具有更广泛的意义。 为了完成双子过程的研究，皮秒弛豫后 卟啉金属烷基自由基笼前体光分解 还将考察络合物和酮亚胺，R2C=C=N-R‘。 为了了解一氧化氮相互作用的生物效应，详细介绍了 模型亚铁血红素的平衡和皮秒动力学研究 将对络合物进行研究。结构和环境对NO的影响 亚铁血红素结合动力学和平衡以及亚铁血红素-一氧化氮的形成 将对碱-血红素-NO进行详细研究。PH对NO结合的影响， 近端碱基解离和皮秒NO动力学将用 肌红蛋白和其他血红素蛋白。 设计用于模拟蛔虫、血红蛋白和蛋白质的新模型系统 将制备具有高极性口袋的过氧化物酶。这些型号 将提供当前讨论中所需的基本结构效果 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.