Characterisation of phosphate binding to mitochondrial and bacterial membrane-bound ATP synthase by studies of inhibition with 4-chloro-7-nitrobenzofurazan
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چکیده
منابع مشابه
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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15 صفحه اولGenes for bacterial and mitochondrial ATP synthase.
The structures of the ATP synthases in bacteria and mitochondria are very similar (for reviews see Senior, 1979; Fillingame, 1981 ; Racker, 1981 ; Walker et al., 1982). They are membrane-bound enzymes composed of two distinct domains: a domain called F, which is buried in the membrane and attached to it a domain known as F, which lies outside the membrane (see Fig. 1). F, is composed of five di...
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15 صفحه اولSynthesis of 4-aryloxy-7-nitrobenzofurazan Derivatives from 4-chloro-7-nitrobenzofurazan and Various Phenoxide Anions (Including Pharmaceuticals) in the Presence of Crown Ethers
4-Chloro-7-nitrobenzofurazan reacts by nucleophilic substitution with phenoxide anions derived from estriol (2c), ethynylestradiol (2d), phenol (3e), guaiacol (3f ), 2,6dimethoxyphenol (3g), eugenol (3h), isoeugenol (3i), the cytostatic Etoposide (4), and Reichardt’s betaine (5) in the presence of crown ethers a¬ording the corresponding 4-aryloxy7-nitrobenzofurazan derivatives 6c, 6d, 7e { 7i, ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1986
ISSN: 0014-5793
DOI: 10.1016/0014-5793(86)81195-4