FLAVIN-PROTEIN INTERACTIONS IN FLAVOENZYME CATALYSIS

我们计划扩展我们的研究的离子强度依赖的黄素氧还蛋白 电子转移反应，以包括其他黄素（以测试一般性 我们的结论），二氯黄素类似物蛋白质（这些是感兴趣的 因为我们能够分离复合物形成的速率常数， 电子转移，这是正常黄素氧还蛋白无法达到的）， 完全还原的蛋白质的反应（以观察离子强度效应是否取决于 也因为这种物质的许多反应是 在高离子强度下太快而无法测量，但在低离子强度下应可测量 实力 我们还计划继续我们的工作对黄素-细胞色素c-细胞色素氧化酶 系统 特别感兴趣的是离子强度依赖性的调查 检查电荷相互作用，细胞色素c浓度依赖性（以 检查高亲和力和低亲和力两者的占据的动力学效应。 氧化酶上的亲和结合位点），依赖于 还原氧化酶（以检查电子进入氧化酶的速率）。 各种氧化还原位点，即α、α 3和铜），以及CO配位的影响 氧化酶（它改变了各个位点的氧化还原电位。

We plan to extend our studies of the ionic strength dependence of flavodoxin electron transfer reactions to include other flavodoxins (to test the generality of our conclusions), dichloroflavin analog protins (these are of interest because we are able to separate the rate constants for complex formation and electron transfer, which are inaccessible with the normal flavodoxin) and reactions of the fully-reduced protein (to see if ionic strength effects depend on oxidation state and also because many of the reactions of this species are too fast to measure at high ionic strength but should be measurable at low ionic strength. We also plan to continue our work on the flavin-cytochrome c-cytochrome oxidase system. Of particular interest are investigations of ionic strength dependence to examine charge interactions, of cytochrome c concentration dependence (to examine the kinetic effects of occupation of both the high affinity and low affinity binding sites on the oxidase), of dependence on the initial state of reduction of the oxidase (to examine the rates of entry of electrons into the various redox sites, i.e. a, a3 and copper), and of the effects of CO liganding of the oxidase (which changes the redox potentials of the various sites.