Investigations on nucleotide binding sites of isolated chloroplast ATPase by modification with 7-chloro-4-nitrobenzofurazan

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7-Chloro-4-nitrobenzofurazan inactivates chloroplast H(2+)-ATPase by modification of different tyrosines, depending on the presence of ATP.

The addition of 7-chloro-4-nitrobenzofurazan (NBD) to isolated CF1 at pH 7.5 leads to one tyrosine-bound NBD molecule per CF1 in one of the three beta-subunits, concomitantly with the inhibition of the ATPase activity. Addition of ADP prior to NBD-incubation protected the ATPase activity and reduced binding of NBD to beta-subunits. The addition of MgATP prior to modification did not result in p...

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Characterization of nucleotide-binding sites on the chloroplast coupling factor 1 using two photolabile analogs.

Nucleotide-binding sites on the chloroplast coupling factor 1 (CF1) have been probed using two photoreactive ADP analogs: 2-azido-ADP (2-N3-ADP) and 2',3'-O-(4-benzoyl)benzoyl-ADP (Bz-ADP). Photolabeling of the isolated CF1 with 2-N3-ADP results in incorporation of the analog exclusively into the beta-subunit of the enzyme. The location of the nucleotide-binding site(s) within the beta-subunit ...

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Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.

We have studied the properties of beef heart mitochondrial F1 having inhibitory MgADP bound at one of the three catalytic sites and various levels of occupancy of the three noncatalytic nucleotide sites including zero, two, or three ADP/ATPs or two ADP/ATP plus one GTP. The properties examined include the rate of MgATP-dependent reactivation and the rate of increase in the fraction of F1 contai...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1989

ISSN: 0014-5793

DOI: 10.1016/0014-5793(89)81681-3