Identification of phosphate binding residues of Escherichia coli ATP synthase

被引：27

作者：

Ahmad, Z ^{[1
]}

Senior, AE ^{[1
]}

机构：

[1] Univ Rochester, Dept Biochem & Biophys, Med Ctr, Rochester, NY 14627 USA

来源：

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES | 2005年 / 37卷 / 06期

关键词：

oxidative phosphorylation; ATP synthesis; ATP synthase catalytic site beta E; Pi binding; subdomain; Pi binding residues;

D O I：

10.1007/s10863-005-9486-8

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 [生物物理学];

摘要：

Four positively-charged residues, namely beta Lys-155, beta Arg-182, beta Arg-246 and alpha Arg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site beta E where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of beta Arg-246 is shown to be one important component of Pi binding.

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页码：437 / 440

页数：4

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