The ion channel of the ATP-synthase from chloroplasts.

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作者信息

Grotjohann I, Gräber P

机构信息

Max-Volmer-Institut, Technische Universität Berlin, FRG.

出版信息

J Protein Chem. 1989 Jun;8(3):379-80. doi: 10.1007/BF01674288.

DOI:10.1007/BF01674288

PMID:2477016

Abstract

摘要

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The ion channel of the ATP-synthase from chloroplasts.

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CF0, the proton channel of chloroplast ATP synthase. After removal of CF1 it appears in two forms with highly different proton conductance.CF0，叶绿体ATP合酶的质子通道。去除CF1后，它以两种具有高度不同质子传导率的形式出现。

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Proton flow through the ATP synthase in chloroplasts regulates the distribution of light energy between PS I and PS II.质子通过叶绿体中的ATP合酶流动，调节光能在光系统I和光系统II之间的分配。

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Dye-ligand chromatographic purification of intact multisubunit membrane protein complexes: application to the chloroplast H+-FoF1-ATP synthase.完整多亚基膜蛋白复合物的染料配体色谱纯化：应用于叶绿体H⁺-FoF₁-ATP合酶

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本文引用的文献

Preparation and properties of chloroplasts depleted of chloroplast coupling factor 1 by sodium bromide treatment.用溴化钠处理制备脱耦联因子 1 的叶绿体及性质研究。

Plant Physiol. 1975 Feb;55(2):282-7. doi: 10.1104/pp.55.2.282.

The proteolipid subunit of the chloroplast adenosine triphosphatase complex. Reconstitution and demonstration of proton-conductive properties.叶绿体腺苷三磷酸酶复合物的蛋白脂质亚基。质子传导特性的重建与证明。

J Biol Chem. 1980 Nov 25;255(22):10638-43.

Structure of the ATP-synthase from chloroplasts and mitochondria studied by electron microscopy.通过电子显微镜研究叶绿体和线粒体中ATP合酶的结构。

Z Naturforsch C J Biosci. 1988 Mar-Apr;43(3-4):219-25. doi: 10.1515/znc-1988-3-412.

Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.细菌腺苷5'-三磷酸合酶（F1F0）：F0复合物的纯化与重组及其亚基的生化和功能特性

Microbiol Rev. 1987 Dec;51(4):477-97. doi: 10.1128/mr.51.4.477-497.1987.

The proton channel, CF0, in thylakoid membranes. Only a low proportion of CF1-lacking CF0 is active with a high unit conductance (169 fS).类囊体膜中的质子通道CF0。只有一小部分缺乏CF1的CF0具有高单位电导率（169飞西门子）且处于活性状态。

Eur J Biochem. 1986 Nov 3;160(3):627-34. doi: 10.1111/j.1432-1033.1986.tb10084.x.

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