The possible role of tightly bound adenine nucleotides in oxidative and photosynthetic phosphorylation
Author:
Publisher
Wiley
Subject
General Medicine
Reference37 articles.
1. Tight binding of adenine nucleotides to beef-heart mitochondrial ATPase
2. and in “Membrane Proteins in Transport and Phosphorylation,” and (Eds.). North Holland Publishing Co., Amsterdam, p. 137 (1974).
3. Tightly bound adenine nucleotide in bacterial membrane ATPase
4. in “Dynamics of Energy-Transducing Membranes,” and (Eds.). Elsevier, Amsterdam, p. 1 (1974).
5. A New Concept for Energy Coupling in Oxidative Phosphorylation Based on a Molecular Explanation of the Oxygen Exchange Reactions
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1. Rotary Movements within the ATP Synthase do not Constitute an Obligatory Element of the Catalytic Mechanism;IUBMB Life (International Union of Biochemistry and Molecular Biology: Life);2003-08-01
2. 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
3. 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
4. Analysis of the Nucleotide Binding Sites of ATP Synthase and Consequences for the Catalytic Mechanism;Frontiers of Cellular Bioenergetics;1999
5. Inhibition of mitochondrial F1-ATPase activity by binding of (2-azido-)ADP to a slowly exchangeable non-catalytic nucleotide binding site;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1992-08
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