ISOLATION AND CHARACTERIZATION OF A FUNCTIONAL ALPHA-BETA HETERODIMER FROM THE ATP SYNTHASE OF RHODOSPIRILLUM-RUBRUM

被引：14

作者：

ANDRALOJC, PJ ^{[1
]}

HARRIS, DA ^{[1
]}

机构：

[1] UNIV OXFORD,DEPT BIOCHEM,S PARKS RD,OXFORD OX1 3QU,ENGLAND

来源：

FEBS LETTERS | 1992年 / 310卷 / 02期

关键词：

RHODOSPIRILLUM-RUBRUM; ENZYME RECONSTITUTION; ATP SYNTHASE; F(1)-ATPASE; SUBUNIT INTERACTIONS; HETERODIMER;

D O I：

10.1016/0014-5793(92)81326-H

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An alpha-beta heterodimer of the F1-ATPase of Rhodospirillum rubrum was isolated by extraction of chromatophores with LiCl. Each alpha-beta heterodimer contains one tightly bound ADP, which is released upon removal of medium Mg2+. The dimer can be reversibly dissociated by removal of Mg2+-ions. The alpha-beta heterodimer restores both ATP-synthetic and -hydrolytic activities to LiCl-treated chromatophores, saturation being achieved at approximately 2 mmol alpha-beta . mol BChl-1. The heterodimer itself hydrolyses Mg-ATP with an activity distinct from RF1, being unaffected by azide or sulphite ions. The V(max) and K(m) (ATP) for this Mg2+-dependent activity were 110 +/- 10 nmol . min-1 . mg protein-1 and 100 +/- 30-mu-M, respectively. The K(m) did not differ significantly from that of RF1.

引用

页码：187 / 192

页数：6

共 43 条

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