STUDIES OF O2 ACTIVATION BY MOSSBAUER SPECTROSCOPY

通过穆斯鲍尔光谱研究 O2 活化

• 批准号: 3271260
• 负责人: ECKARD MUNCK
• 金额: $ 15.32万
• 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 1991-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3271260
• 关键词: Mossbauer spectrometry; bacterial proteins; electron spin resonance spectroscopy; electron transport; enzyme mechanism; enzyme structure; enzyme substrate complex; hemoprotein; iron; kidney; metalloenzyme; oxygenases; sulfur compounds

The research proposed here seeks to determine the electronic structures of some iron containing enzymes using Mossbauer spectroscopy and electron paramagnetic resonance. The experiments include: 1) Further studies of the cluster structures and reaction mechanism of aconitase, a key enzyme in the citric acid cycle. 2) Continuation of research into the nature of the active sites of dioxygenases. These enzymes cleave catechols by oxygen insertion and are of major importance in the biodegradation of aromatic compounds in the biosphere. 3) Continuation of Mossbauer studies of cytochrome oxidase, the terminal enzyme of the respiratory chain. The a3-site of the enzyme, the locus of oxygen reduction, will be studied with enzymes isolated from beef heart mitochondria, Thermus thermophilus and Nitrosomonas europeae. 4) It is also proposed to study a lignin-degrading enzyme from the fungus P. chrysosporium.

这里提出的研究旨在确定的电子结构