Severe MgADP Inhibition of Bacillus subtilis F1-ATPase Is Not Due to the Absence of Nucleotide Binding to the Noncatalytic Nucleotide Binding Sites

被引：6

作者：

Ishikawa, Toru ^{[1
]}

Kato-Yamada, Yasuyuki ^{[1
,2
]}

机构：

[1] Rikkyo Univ, Dept Life Sci, Toshima Ku, Tokyo 171, Japan

[2] Rikkyo Univ, Res Ctr Life Sci, Toshima Ku, Tokyo 171, Japan

来源：

PLOS ONE | 2014年 / 9卷 / 09期

关键词：

MITOCHONDRIAL ADENOSINE-TRIPHOSPHATASE; APPARENT NEGATIVE COOPERATIVITY; ALPHA(3)BETA(3)GAMMA COMPLEX; CATALYTIC SITE; KINETIC MECHANISM; ATP SYNTHASE; PS3; SUBSTITUTION; HYDROLYSIS; ROTATION;

D O I：

10.1371/journal.pone.0107197

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

F-1-ATPase from Bacillus subtilis (BF1) is severely suppressed by the MgADP inhibition. Here, we have tested if this is due to the loss of nucleotide binding to the noncatalytic site that is required for the activation. Measurements with a tryptophan mutant of BF1 indicated that the noncatalytic sites could bind ATP normally. Furthermore, the mutant BF1 that cannot bind ATP to the noncatalytic sites showed much lower ATPase activity. It was concluded that the cause of strong MgADP inhibition of BF1 is not the weak nucleotide binding to the noncatalytic sites but the other steps required for the activation.

引用

页数：5

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