Kinetic studies on rat liver and beef heart mitochondrial ATPase. Evidence for nucleotide binding at separate regulatory and catalytic sites.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
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4. Differential Effects of Adenylyl Imidodiphosphate on Adenosine Triphosphate Synthesis and the Partial Reactions of Oxidative Phosphorylation
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1. 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
2. ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas;Microbiology and Molecular Biology Reviews;2008-12
3. The α3β3γ Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the βT165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover;Journal of Biological Chemistry;1996-11
4. Lowered Temperature or Binding of Pyrophosphate to Sites for Noncatalytic Nucleotides Modulates the ATPase Activity of the Beef Heart Mitochondrial F1-ATPase by Decreasing the Affinity of a Catalytic Site for Inhibitory MgADP;Biochemistry;1994-12-01
5. Hysteretic inhibition of the bovine heart mitochondrial F1-ATPase is due to saturation of noncatalytic sites with ADP which blocks activation of the enzyme by ATP.;Journal of Biological Chemistry;1994-01
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