ELECTRON TRANSPORT & ENERGY CONSERVATION IN MITOCHONDRIA

电子传输

• 批准号: 3285060
• 负责人: JOHN C SALERNO
• 金额: $ 5.66万
• 依托单位: RENSSELAER POLYTECHNIC INSTITUTE
• 依托单位国家: 美国
• 财政年份: 1986
• 资助国家: 美国
• 起止时间: 1986-01-01 至 1988-12-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3285060
• 关键词: Raman spectrometry; bioenergetics; conformation; cytochromes; electron nuclear double resonance spectroscopy; electron spin resonance spectroscopy; electron transport; hydrogen transport; laboratory rat; membrane potentials; membrane structure; mitochondria; mitochondrial membrane; oxidation reduction reaction; pigeons; thermodynamics

The proposal outlines a series of investigations which aim to provide information essential to the understanding of electron transfer and energy transduction in the cytochrome bc1 region of the mitochondrial respiratory chain. The proposal utilizes a variety of biophysical and biochemical approaches to provide structural and thermodynamic information and to investigate the possibility of functional interactions between components. Structural information will be obtained using oriented multilayer and paramagnetic probes approaches. Oxidation/reduction titrations will be performed under a variety of conditions to evaluate the possibility of cooperativity between various components and to study the causes and implications of spectral shifts. This area is important because mitochondria are the major source of energy for animal cells, because related electron transfer systems are important in a wide variety of systems not directly connected to energy transduction (e.g., steroid hormone synthesis, macrophage peroxide production) and because bacterial and fungal respiration utilize similar respiratory chains.

该提案概述了一系列旨在提供的调查 了解电子传输和能量至关重要的信息 线粒体呼吸的细胞色素BC1区域的转导 链。 该提案利用各种生物物理和生化 提供结构和热力学信息的方法 研究组件之间功能相互作用的可能性。 结构信息将使用定向的多层和 顺磁性探针接近。 氧化/还原滴定将是 在各种条件下进行 各个组成部分之间的合作性并研究原因和 光谱转移的含义。 这个区域很重要，因为 线粒体是动物细胞的主要能量来源，因为 相关的电子传输系统在各种各样的 系统未直接连接到能量转导的系统（例如类固醇 激素合成，巨噬细胞过氧化物的产生）和由于细菌 和真菌呼吸利用类似的呼吸链。

项目成果

Heme-copper and heme-heme interactions in the cytochrome bo-containing quinol oxidase of Escherichia coli.

大肠杆菌细胞色素 bo 羟基氧化酶中血红素-铜和血红素-血红素相互作用。

• 发表时间: 1990
• 期刊: The Journal of biological chemistry
• 作者: Salerno,JC;Bolgiano,B;Poole,RK;Gennis,RB;Ingledew,WJ
• 通讯作者: Ingledew,WJ

Electron nuclear double resonance (ENDOR) of the Qc.- ubisemiquinone radical in the mitochondrial electron transport chain.

线粒体电子传递链中 Qc.-泛半醌自由基的电子核双共振 (ENDOR)。

• DOI: 10.1021/bi00482a006
• 发表时间: 1990
• 期刊: Biochemistry
• 影响因子: 2.9
• 作者: Salerno,JC;Osgood,M;Liu,YJ;Taylor,H;Scholes,CP
• 通讯作者: Scholes,CP

Orientation of the haems of the ubiquinol oxidase:O2 reductase, cytochrome bo of Escherichia coli.

泛醇氧化酶：O2 还原酶、大肠杆菌细胞色素 bo 的血红素方向。

• DOI: 10.1111/j.1432-1033.1991.tb16082.x
• 发表时间: 1991
• 期刊: European journal of biochemistry
• 作者: Salerno,JC;Ingledew,WJ
• 通讯作者: Ingledew,WJ

The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli.

大肠杆菌“原位”泛醇氧化酶细胞色素 bd 的三个血红素的方向。

• DOI: 10.1042/bj2820255
• 发表时间: 1992
• 期刊: The Biochemical journal
• 作者: Ingledew,WJ;Rothery,RA;Gennis,RB;Salerno,JC
• 通讯作者: Salerno,JC

Stabilized ubisemiquinone in reconstituted succinate ubiquinone reductase.

重构琥珀酸泛醌还原酶中稳定的泛半醌。

• DOI: 10.1016/s0006-291x(87)80512-0
• 发表时间: 1987
• 期刊: Biochemical and biophysical research communications
• 影响因子: 3.1
• 作者: Xu,Y;Salerno,JC;Wei,YH;King,TE
• 通讯作者: King,TE