Competition between ADP and nucleotide analogues to occupy regulatory site(s) related to hysteretic inhibition of mitochondrial F1-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. "Hysteretic" behavior and nucleotide binding sites of pig heart mitochondrial F1 adenosine 5'-triphosphatase
2. Slow Transitions and Hysteretic Behavior in Enzymes
3. Optimization of the purification of mitochondrial F1-adenosine triphosphatase
4. PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
5. Pig heart mitochondrial ATPase : properties of purified and membrane-bound enzyme
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2. The Binding Mechanism of the Yeast F1-ATPase Inhibitory Peptide;Journal of Biological Chemistry;2005-03
3. Functional transitions of F0F1-ATPase mediated by the inhibitory peptide IF1 in yeast coupled submitochondrial particles;European Journal of Biochemistry;2004-05
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. One of the non-exchangeable nucleotides of the mitochondrial F1-ATPase is bound at a β-subunit: evidence for a non-rotatory two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1999-06
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