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.
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页码：187 / 192
页数：6
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