ELECTRONIC STRUCTURE OF FE-OXO AND MN-OXO COMPLEXES

FE-OXO 和 MN-OXO 配合物的电子结构

• 批准号: 3302317
• 负责人: Louis Noodleman
• 金额: $ 9.51万
• 依托单位: SCRIPPS RESEARCH INSTITUTE, THE
• 依托单位国家: 美国
• 财政年份: 1991
• 资助国家: 美国
• 起止时间: 1991-05-01 至 1996-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3302317
• 关键词: Mossbauer spectrometry; acid phosphatase; active sites; biomagnetism; catalyst; chemical models; electron spin resonance spectroscopy; electronic spectra; enzyme model; iron oxide; iron sulfur protein; manganese; metal complex; metalloproteins; methane monooxygenase; quantum chemistry; ribonucleotide reductase

This proposal involves the use of quantum mechanical calculations and subsequent analysis to examine the electronic structure of dinuclear and polynuclear Fe-O complexes and Mn-O complexes as relevant models for active sites of metalloprotein systems. Fe-O complexes are found in: (a) ribonucleotide reductase, (b) methane monooxygenase, (c) purple acid phosphatases,and (d) hemerythrin. A polynuclear Mn-O complex occurs at the active site in the oxygen evolving complex of photosystem II. All of our calculations will be of the Xalpha or local spin density self consistent field type. We will systematically study relevant model complexes as a function of oxidation state, coordination geometry, and binding of substrate ligands or reaction intermediates. The calculations will be compared with experimental results by magnetic susceptibility, and by Mossbauer, electron spin resonance and/or optical spectroscopies for proteins and synthetic analogues. Further, we will examine electron density distributions and spin density distributions in some detail since these features should be closely associated with catalytic mechanism. Qualitative and quantitative ligand binding energetics will also be explored. Our goal is to relate predicted and experimental properties as well as to gain insight into catalytic function and regulation in these enzymes.

该建议涉及使用量子机械 计算和后续分析以检查电子 双核和多核Fe-O复合物以及MN-O的结构 复合物作为金属蛋白活性位点的相关模型 系统。 Fe-O复合物在以下位置中找到：（a）核糖核苷酸 还原酶，（b）甲烷单加氧酶，（c）紫色酸 磷酸酶和（d）hymerythrin。 多核MN-O复合物 发生在氧气进化的复合物中的活性位点 光系统II。 我们所有的计算将是Xalpha或本地旋转的 密度自我一致的场类型。 我们将系统地学习 相关模型复合物作为氧化状态的函数， 协调几何形状和底物配体的结合或 反应中间体。 将将计算与 通过磁化率和 Mossbauer，电子自旋共振和/或光谱镜 用于蛋白质和合成类似物。 此外，我们将检查 电子密度分布和旋转密度分布 一些细节，因为这些功能应密切相关 具有催化机制。 定性和定量配体 还将探索绑定能量学。 我们的目标是联系 预测和实验特性以及获得洞察力 这些酶中的催化功能和调节。