Rate of chase-promoted hydrolysis of ATP in the high affinity catalytic site of beef heart mitochondrial ATPase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference17 articles.
1. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site.
2. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.
3. Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodiimide and oligomycin: relationship to ATP synthesis.
4. Reaction mechanism of the membrane-bound ATPase of submitochondrial particles from beef heart.
5. Energy-dependent dissociation of ATP from high affinity catalytic sites of beef heart mitochondrial adenosine triphosphatase.
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1. Structure and Mechanism of F0F1-Type ATP Synthases and ATPases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Origin of apparent negative cooperativity of F1-ATPase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2003-10
3. The molecular mechanism of ATP synthesis by F1F0-ATP synthase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2002-02
4. Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05
5. Analysis of the Nucleotide Binding Sites of ATP Synthase and Consequences for the Catalytic Mechanism;Frontiers of Cellular Bioenergetics;1999
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