Study of the protein-ubiquinone interaction in succinate-cytochrome C reductase with azido-ubiquinone derivatives |
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Authors: | C A Yu L Q Gu L Yu |
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Affiliation: | Department of Biochemistry, Oklahoma State University Stillwater, OK 74078 USA |
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Abstract: | Several azido-ubiquinones have been synthesized for the study of protein-ubiquinone interaction in succinate-cytochrome reductase. In the absence of light, azido-ubiquinones are partially effective in restoring enzymatic activity to ubiquinone- and phospholipid-depleted reductase and the binding of azido-ubiquinones can be partially reversed by 5-(10-bromodecyl)-ubiquinone. When 2-azido-3-methoxy-5-geranyl-6-methyl-1,4-benzoquinone reactivated reductase is illuminated with long wavelength UV light, a complete and irreversible inhibition is observed. This specific photo-inactivation, exerted only by 2-azido-3-methoxy-5-geranyl-6-methyl-1,4-benzoquinone, and not by other azido-ubiquinone derivatives, is evidence for the existence of a specific benzoquinone ring binding site in the enzyme. |
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Keywords: | PL phospholipid Q ubiquinone 2,3-dimethoxy-6-methyl-1,4-benzoquinone 2,3-dimethoxy-6-methyl-5-(3-methylbutyl)-1,4-benzoquinone 2-azido-3-methoxy-6-methyl-1,4-benzoquinone 2,3-dimethoxy-6-methyl-5-(10-bromodecyl)-1,4-benzoquinone 2,3-dimethoxy-5-geranyl-6-methyl-1,4-benzoquinone 2-azido-3-methoxy-5-geranyl-6-methyl-1,4-benzoquinone 3-azido-2-methoxy-5-geranyl-6-methyl-1,4-benzoquinone 6-azido-5-decyl-2,3-dimethoxy-1,4-benzoquinone |
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