Substitution of βGlu201 in the α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 Increases the Affinity of Catalytic Sites for Nucleotides-Reference-Cited by-同舟云学术

Substitution of βGlu201 in the α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 Increases the Affinity of Catalytic Sites for Nucleotides

Published:2000-04 Issue:14 Volume:275 Page:10057-10063
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ren Huimiao,Allison William S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE

2. Catalytic mechanism of F1-ATPase

3. Slow binding of ATP to noncatalytic nucleotide binding sites which accelerates catalysis is responsible for apparent negative cooperativity exhibited by the bovine mitochondrial F1-ATPase.

4. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

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1. Characteristics of protection by MgADP and MgATP of α3β3Γ subcomplex of thermophilic Bacillus PS3 βY341W-mutant F1-ATPase from inhibition by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole support a Bi-site mechanism of catalysis;Biochemistry (Moscow);2011-11

2. Probes of inhibition of Escherichia coli F1-ATPase by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole in the presence of MgADP and MgATP support a bi-site mechanism of ATP hydrolysis by the enzyme;Biochemistry (Moscow);2010-03

3. Modulation of nucleotide binding to the catalytic sites of thermophilic F1-ATPase by the ε subunit: Implication for the role of the ε subunit in ATP synthesis;Biochemical and Biophysical Research Communications;2009-12

4. Stepwise Propagation of the ATP-induced Conformational Change of the F1-ATPase β Subunit Revealed by NMR;Journal of Biological Chemistry;2009-01

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