Constant c10 Ring Stoichiometry in the Escherichia coli ATP Synthase Analyzed by Cross-Linking

被引：34

作者：

Ballhausen, Britta ^{[1
]}

Altendorf, Karlheinz ^{[1
]}

Deckers-Hebestreit, Gabriele ^{[1
]}

机构：

[1] Univ Osnabruck, Fachbereich Biol Chem, Arbeitsgrp Mikrobiol, D-49069 Osnabruck, Germany

来源：

JOURNAL OF BACTERIOLOGY | 2009年 / 191卷 / 07期

关键词：

PROTON-TRANSLOCATING ATPASE; SUBUNIT C OLIGOMER; H+/ATP RATIO; F1F0; ATPASE; ROTOR RING; F-0; SECTOR; MEMBRANE; EXPRESSION; GENES; MODEL;

D O I：

10.1128/JB.01390-08

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The subunit c stoichiometry of Escherichia coli ATP synthase was studied by intermolecular cross-linking via oxidation of bi-cysteine-substituted subunit c (cA21C/cM65C). Independent of the carbon source used for growth and independent of the presence of other F0F1 subunits, an equal pattern of cross-link formation stopping at the formation of decamers was obtained.

引用

页码：2400 / 2404

页数：5

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