O2 Activation by Mossbauer Spectroscopy

通过穆斯堡尔光谱法激活 O2

• 批准号: 7217892
• 负责人: ECKARD MUNCK
• 金额: $ 29.65万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1990
• 资助国家: 美国
• 起止时间: 1990-05-01 至 2008-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7217892
• 关键词: Active Sites; Cells; Complement; Complex; Cytochrome P450; Electron Spin Resonance Spectroscopy; Electronics; Enzymes; Escherichia coli; Iron; Magnetometries; Methane hydroxylase; Modeling; Mossbauer Spectroscopy; Nonheme Iron Proteins; Oxygen; Protein Overexpression; Proteins; Research; Ribonucleotide Reductase; Site; Squid; Structure; Study models; Techniques; density; desaturase; enzyme model; ferryl iron; insight; theories; thermophilic bacteria

DESCRIPTION (provided by applicant): This proposal seeks to elucidate the structure and function of iron-containing enzymes involved in oxygen activation. Moreover, it is proposed to study a variety of Fe(IV) containing synthetic compounds that mimic structural and electronic features of the active sites of the enzymes under study. Further, it is proposed to study the Mossbauer spectra of proteins in overexpressing E. coli cells. The experimental techniques employed are Mossbauer spectroscopy, Electron paramagnetic resonance (EPR) and SQUID magnetometry. It is also proposed to study high-valent Fe(IV) sites of proteins and model complexes with density functional theory. (1) Studies of the diiron proteins methane monooxygenase, ribonucleotide reductase, delta9 desaturase and phenolhydroxylase will be continued. (2) This research will be complemented by studies of model complexes to gain insight into the electronic structure of the active sites of the enzymes. (3) Whole-cell studies of iron containing proteins overexpressed in E. coli will be continued. (4) The Mossbauer and EPR spectra of compound I of cytochrome P450 isolated from a thermophilic bacterium will be studied. (5) Mossbauer and EPR studies of four non-heme iron proteins suspected to pass in their catalytic cycles through an Fe(IV)=O intermediate will be performed. (6) Iron(IV) sites occurring in enzymes and model complexes will be investigated with density functional theory.

描述（由申请人提供）：本提案旨在阐明参与氧活化的含铁酶的结构和功能。此外，建议研究各种含Fe（IV）的合成化合物，其模拟所研究的酶的活性位点的结构和电子特征。此外，建议研究蛋白质的穆斯堡尔谱过表达E。大肠杆菌细胞。所采用的实验技术是穆斯堡尔谱，电子顺磁共振（EPR）和SQUID磁强计。 并提出用密度泛函理论研究蛋白质和模型配合物的高价Fe（IV）位点。 (1)对二铁蛋白甲烷单加氧酶、核糖核苷酸还原酶、δ 9去饱和酶和苯酚羟化酶的研究将继续进行。 (2)这项研究将通过模型复合物的研究来补充，以深入了解酶活性位点的电子结构。 (3)大肠杆菌中过表达的含铁蛋白的全细胞研究。大肠杆菌的感染情况。 (4)本文研究了从嗜热菌中分离的细胞色素P450化合物Ⅰ的穆斯堡尔谱和EPR谱。 (5)穆斯堡尔谱和EPR研究四个非血红素铁蛋白怀疑通过其催化循环通过Fe（IV）=O中间体将进行。 (6)铁（IV）网站发生在酶和模型复合物将与密度泛函理论研究。