RESPIRATORY PROTEIN COMPLEXES

呼吸蛋白复合物

• 批准号: 2183580
• 负责人: James D. Satterlee
• 金额: $ 13.2万
• 依托单位: WASHINGTON STATE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1992
• 资助国家: 美国
• 起止时间: 1992-09-30 至 1996-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2183580
• 关键词: covalent bond; cytochrome c; enzyme activity; enzyme complex; enzyme mechanism; iron compounds; isozymes; nuclear magnetic resonance spectroscopy; peroxidases; respiratory protein; yeasts

Using the results from our previous work on yeast cytochrome c peroxidase (CcP) complexes, this proposal reflects the comments of the previous NIH Study Section which recommended a proposal tightly focused on NMR studies of noncovalent CcP/cytochrome c complexes. In this proposal we intend to focus on comparative studies of a nonphysiological type of CcP complex: between CcP and horse cytochrome c; and a physiological type of CcP complex: between CcP and its natural redox partner yeast iso- 1 cytochrome c. This discrimination of complex type is based upon results from our work during the past three years, which segregate themselves along species-specific lines. One of our most interesting results during this time has been the resolution of free and bound ferricytochrome c resonances in NMR spectra of CcP/ferricytochrome c noncovalent complexes. We propose to further characterize these complexes by NMR spectroscopy, elucidate the complex dissociation rate constants and determine the effects on cytochrome c NMR spectra of forming complexes with native, wild-type CcP (a ferric, high-spin heme protein), and as well, with the oxidized intermediates, CcP-I (compound-I) and CcP-II (compound-II), and cyanide-inhibited CcP (CcPCN). NMR detection of effects of complex formation upon CcP will be attempted using CcPCN in combination with ferro- and ferricytochromes c.

利用我们之前对酵母细胞色素c过氧化物酶的研究结果