Inhibitory Mg-ADP-fluoroaluminate complexes bound to catalytic sites of F1-ATPases:: Are they ground-state or transition-state analogs?

被引：9

作者：

Allison, WS ^{[1
]}

Ren, HM ^{[1
]}

Dou, C ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

来源：

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES | 2000年 / 32卷 / 05期

关键词：

F-1-ATPase; transition-state analog; ground-state analog; rotational catalysis;

D O I：

10.1023/A:1005677310791

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Schemes are proposed for coupling sequential opening and closing the three catalytic sites of Fl to rotation of the gamma subunit during ATP synthesis and hydrolysis catalyzed by the FoF1-ATP synthase. A prominent feature of the proposed mechanisms is that the transition state during ATP synthesis is formed when a catalytic site is in the process of closing and that the transition state during ATP hydrolysis is formed when a catalytic site is in the process of opening. The unusual kinetics of formation of Mg-ADP-fluoroaluminate complexes in one or two catalytic sites of nucleotide-depleted MF1 and wild-type and mutant alpha (3)beta (3)gamma subcomplexes of TF1 are also reviewed. From these considerations, it is concluded that Mg-ADP-fluoroaluminate complexes formed at catalytic sites of isolated F-1-ATPases or F-1 in membrane-bound FoF1 are ground-state analogs.

引用

页码：531 / 538

页数：8

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