BIOLOGICAL OXIDATION MECHANISMS

生物氧化机制

• 批准号: 3268236
• 负责人: VINCENT MASSEY
• 金额: $ 28.27万
• 依托单位: UNIVERSITY OF MICHIGAN AT ANN ARBOR
• 依托单位国家: 美国
• 财政年份: 1978
• 资助国家: 美国
• 起止时间: 1978-09-01 至 1988-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3268236
• 关键词: Escherichia coli; X ray crystallography; aminoacid oxidase; charge transfer complex; chemical reaction; cofactor; electron transport; enzyme model; enzyme structure; enzyme substrate complex; flavins; flavoproteins; fluorescence spectrometry; hydroxybenzoate; hydroxylation; lactate dehydrogenases; oxidation; oxygenases; protonation; radiotracer; spectrometry

The main aim of the research project is an understanding of the chemical reactivity of flavin coenzymes and how this reactivity is used and controlled in biological systems. The methods of approach will be the study of specific enzymes representative of the various classes of flavoproteins and studies of model systems. Considerable use will be made of steady state kinetics coupled with rapid reaction kinetic studies, and of the technique of replacing the natural coenzymes of falvoproteins with synthetic flavins, in order to test hypothetical schemes and to probe the nature of the environment immediately around the flavin. The latter is particularly important in providing information about the active site region in proteins where the structure is not available from X-ray crystallography. We also plan to undertake the amino acid sequence of L-lactate oxidase in order to aid in the crystallographic determination of its three-dimensional structure.

研究项目的主要目的是了解化学物质 黄素辅酶的反应性以及如何使用这种反应性和 在生物系统中控制。 方法的方法将是 代表各类的特定酶的研究 黄素蛋白和模型系统的研究。 将大量使用 稳态动力学以及快速反应动力学研究和 用替代水voprotein的天然辅酶的技术 合成黄素，以测试假设方案并探测 立即在黄素周围的环境的性质。 后者是 在提供有关活动网站的信息方面特别重要 蛋白质中的区域，该区域无法从X射线 晶体学。 我们还计划进行氨基酸序列 L乳酸氧化酶，以帮助确定 它的三维结构。