Demonstration of two exchangeable non-catalytic and two cooperative catalytic sites in isolated bovine heart mitochondrial F1, using the photoaffinity labels [2-3H]8-azido-ATP and [2-3H]8-azido-ADP
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference46 articles.
1. CHEMICAL PROBES OF THE MITOCHONDRIAL ATP SYNTHESIS AND TRANSLOCATION
2. An Electron Microscopic Approach to the Quaternary Structure of Mitochondrial F1-ATPase
3. Use of monoclonal antibodies in immuno-electron microscopy for the determination of subunit stoichiometry in oligomeric enzymes
4. The number and localisation of adenine nucleotide-binding sites in beef-heart mitochondrial ATPase (F1) determined by photolabelling with 8-azido-ATP and 8-azido-ADP
5. Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.
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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. FSBA modifies both α- and β-subunits of F1 specifically and can be bound together with AXP at the same α-subunit;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1997-01
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