8-Azido-adenosine 5′-triphosphate as a Photoaffinity Label for Bacterial F1 ATPase
TLDR
8-Azido-adenosine 5'-triphosphate (n83ATP) is a suitable photoaffinity label for F1 ATPase from Micrococcus luteus and n83AMP, a cooperativity of the beta subunits carrying nucleotide binding sites is suggested.Abstract:
1. 8-Azido-adenosine 5'-triphosphate (n83ATP) is a suitable photoaffinity label for F1 ATPase from Micrococcus luteus. The nucleotide is a substrate in the presence of bivalent cations and inhibits the enzyme irreversibly upon irradiation with ultraviolet light above 300 nm. 2. More than 80% of the label is covalently bound to the beta subunits in the presence of bivalent cations. Labeling and inactivation is decreased by protection with ADP, ATP or adenyl-5'-yl imidodiphosphate. To a much smaller degree the alpha subunits also become labeled. 3. n83AMP does not specifically bind to the beta subunits upon irradiation. Like n83ATP and n83ADP, it also labels the alpha subunits to a small extent. 4. The F1 ATPase is inactivated after a single beta subunit per F1 complex has become labeled. A cooperativity of the beta subunits carrying nucleotide binding sites is suggested.read more
Citations
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The binding change mechanism for ATP synthase — Some probabilities and possibilities
TL;DR: Conformational changes and catalysis, the uniqueness of the ATP synthase structure and the role of unfolded protein structure in mechanism are discussed.
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Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.
M Futai,H Kanazawa +1 more
TL;DR: Resume des informations les plus recentes sur the structure and the fonction du complexe F 0 F 1 des bacteries, informations obtenues principalement sur lecomplexe F0 F 1 d'Escherichia coli.
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Reconstitution of a functional coupling factor from the isolated subunits of Escherichia coli F1 ATPase.
Stanley D. Dunn,M Futai +1 more
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Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases.
Pierre V. Vignais,Michel Satre +1 more
TL;DR: The notion that the proton motive force generated by respiration is required for conformational changes of the F1 sector of the H+-ATPase complex has gained acceptance and is supported by kinetic data and by the demonstration of partial site reactivity in inactivation experiments performed with selective chemical modifiers.
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The synthesis of enzyme-bound ATP by soluble chloroplast coupling factor 1.
R I Feldman,D S Sigman +1 more
TL;DR: The data suggest that acid pH values stimulate Pi binding by increasing the concentration of the H2PO4- species, which has been previously shown to be the form of phosphate that binds to beef heart F1 (33).
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