ATP binding and hydrolysis steps of the uni-site catalysis by the mitochondrial F1-ATPase are affected by inorganic phosphate

被引：0

作者：

Milgrom, Yakov M. ^{[1
]}

机构：

[1] SUNY Upstate Med Univ, Dept Biochem & Mol Biol, Syracuse, NY 13210 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2010年 / 1797卷 / 10期

关键词：

ATP synthase; Uni-site catalysis; Bi-site catalysis; Multi-site catalysis; Phosphate; ESCHERICHIA-COLI F1-ATPASE; ADENINE-NUCLEOTIDE BINDING; BOVINE HEART-MITOCHONDRIA; YEAST F-1 ATPASE; ADENOSINE-TRIPHOSPHATASE; OXIDATIVE-PHOSPHORYLATION; BOUND NUCLEOTIDES; SITE OCCUPANCY; SINGLE-SITE; COOPERATIVE INTERACTIONS;

D O I：

10.1016/j.bbabio.2010.07.010

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：

The effect of inorganic phosphate (P-i) on uni-site ATP binding and hydrolysis by the nucleotide-depleted F-1-ATPase from beef heart mitochondria (ndMF(1)) has been investigated. It is shown for the first time that P-i decreases the apparent rate constant of uni-site ATP binding by ndMF(1) 3-fold with the K-d of 0.38 +/- 0.14 mM. During uni-site ATP hydrolysis, P-i also shifts equilibrium between bound ATP and ADP + P-i in the direction of ATP synthesis with the K-d of 0.17 +/- 0.03 mM. However, 10 mM P-i does not significantly affect ATP binding during multi-site catalysis. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：1768 / 1774

页数：7

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