Reconstitution of succinate-Q reductase. |
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Authors: | C A Yu L Yu T E King |
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Institution: | Laboratory of Bioenergetics and Department of Chemistry State University of New York at Albany Albany, New York 12222, USA |
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Abstract: | Reconstitution of succinate-Q reductase is achieved by admixing soluble succinate dehydrogenase (SDH) and ubiquinone-protein-S (QP-S), a new protein isolated from the soluble cytochrome complex. The reconstituted reductase catalyzes reduction of Q by succinate. The reaction is fully sensitive to thenoyltrifluoroacetone. The reconstituted reductase (same as succinate-cytochrome reductase or submitochondrial particles) does not show “low concentration ferricyanide reductase activity” as soluble dehydrogenase does. In other words, this enzymic site on SDH is occupied by QP-S. When an artificial dye, such as phenazine methosulfate or Wurster's Blue, is used as electron acceptor the rate of oxidation of succinate by SDH is not significantly changed regardless of whether the dehydrogenase is in the free or in the reconstituted succinate-Q reductase forms. |
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Keywords: | HEPES N-2-hydroxyethylpiperazine-N′-2′-ethanesulfonic acid TEMED N N N′ N′-tetramethylenediamine |
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