Resolution of Enzymes Catalyzing Energy-linked Transhydrogenation
نویسندگان
چکیده
منابع مشابه
Resolution of enzymes catalyzing energy-linked transhydrogenation. IV. Reconstitution of adenosine triphosphate-driven transhydrogenation in depleted chromatophores of Rhodospirillum rubrum by the transhydrogenase factor and a soluble oligomycin-insensitive Mg ++ -adenosine triphosphatase.
The catalysis of the energy-linked transhydrogenation reaction of Rhodospirillum rubrum chromatophores is dependent upon a soluble protein, the transhydrogenase factor. This factor can be detached from the chromatophore membrane by the relatively mild procedures of extensive washing, passage of chromatophores through Sephadex G-ZOO, or sedimentation of chromatophores through a dense sucrose sol...
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The effect of pH on the kinetics of the following transhydrogenation reactions catalyzed by energized and nonenergized submitochondrial particles has been studied: NADH leads to 3-acetylpyridine adenine dinucleotide phosphate (AcPyADP), NADH leads to thionicotinamide adenine dinucleotide phosphate (thioNADP), NADPH leads to AcPyADP, and NADPH leads to thioNADP. The effect of membrane energizati...
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1. The ability to phosphorylate ADP during oxidation of NADH by ubiquinone-1 was restored to the NADH-ubiquinone reductase complex by combining the latter with phospholipids and a hydrophobic protein fraction derived from bovine heart mitochondria. 2. Phosphorylation was abolished by rotenone, uncoupling agents, or rutamycin. The efficiency of ATP formation was as high as 0.5 mole per mole of N...
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1. Passage of submitochondrial particles through a Sephadex cc,lumn activated the adenosine triphosphatase activity 5to IO-fold and subsequent treatment with urea removed virtually all ATPase (coupling factor 1). The resulting submitochondrial particles, exposed sequentially to Sephadex and urea (SU-particles), catalyzed the oxidation of succinate but phosphorylation was insignificant. P: 0 rat...
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1. A mitochondrial fraction from beef heart (TU-particles) was shown to confer rutamycin sensitivity to added mitochondrial ATPase (F,). After sonic oscillation at an alkaline pH, the resulting particles (TUA-particles) no longer had this activity. A rutamycin sensitivity factor (FJ, purified from crude preparations of coupling factor 4, restored the capacity of the particles to confer rutamyci...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61989-1