XRAY FLUORESCENCE OF NI CONTAINING CARBON MONOXIDE DEHYDROGENASE ENZYMES

含镍一氧化碳脱氢酶的X射线荧光

• 批准号: 6586683
• 负责人: UWE BERGMANN
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586683
• 关键词: biomaterials; biomedical resource; enzymes; proteins; spectrometry; structural biology

Carbon monoxide dehydrogenases are enzymes in the process of carbon fixation and knowledge of the local electronic and physical structure of the metal clusters in these enzymes is essential for the understanding of the mechanisms of CO oxidation and acetyl-CoA synthesis. The detection of the Kb fluorescence with high energy resolution reveals information about oxidation and spin states of first-row transition metal compounds. We propose to use the spin-state sensitivity of the Kb fluorescence to investigate the CODH enzyme from R. rubrum. to extend the current understanding of the Ni-Fe metal cluster by quantifying the amount of high and low spin Ni present. We plan to use site-selective x-ray absorption to study one of the Ni-Fe centers (Center A, the site of acetyl-CoA synthesis) in C. thermoaceticum CODH to study the ligand environment of Ni(I) and Ni(II) and to determine if CO binds to Ni.

一氧化碳脱氢酶是一种酶， 碳固定和当地电子和物理知识 这些酶中金属簇的结构对于 了解CO氧化和乙酰辅酶A的机制 合成. 高能Kb荧光的探测 分辨率揭示了有关氧化和自旋状态的信息， 第一行过渡金属化合物。 我们建议使用 Kb荧光的自旋态灵敏度来研究CODH R.红色。 为了扩展目前对 通过量化高自旋和低自旋Ni的量的Ni-Fe金属簇 礼物 我们计划使用选址X射线吸收来研究一个 Ni-Fe中心（中心A，乙酰辅酶A合成的位点） C.热醋酸菌CODH来研究Ni（I）和Ni（II）的配体环境 Ni（II），并确定CO是否与Ni结合。