Reconstitution of Succinate-Coenzyme Q Reductase (Complex II) and Succinate Oxidase Activities by a Highly Purified, Reactivated Succinate Dehydrogenase

Reconstitution of succinate-coenzyme Q reductase (complex II) and succinate oxidase activities by a highly purified, reactivated succinate dehydrogenase.

Reconstitution of Sue&ate-Coenzyme Q Reductase (Complex II) and Succinate Oxidase Activities by a Highly Purified, Reactivated Succinate Dehydrogenase*

Succinate dehydrogenase has been isolated in a highly purified form from succinate-coenzyme Q reductase preparations. The enzyme contains 1 mole of covalently bound flavin, 8 g atoms of iron, and 8 moles of acid-labile sulfide per 150,000 g of protein. It catalyzes succinate oxidation in the presence of phenazine methosulfate as electron acceptor at a rate of 26 to 32 pmoles per min X mg of pro...

Alternative splicing isoform in succinate dehydrogenase complex, subunit C causes downregulation of succinate-coenzyme Q oxidoreductase activity in mitochondria

Mitochondrial succinate dehydrogenase (SDH) is localized to the inner mitochondrial membrane and is responsible for the redox of succinic acid. SDH is a tetrameric iron-sulfur flavoprotein of the tricarboxylic acid cycle and respiratory chain. The SDH complex, subunit C (SDHC) transcript has deletion-type alternative splicing sites. Generally, alternative splicing produces variant proteins and ...

Studies on Succinate Dehydrogenase

1. Succinate dehydrogenase flavocoenzyme (“SD-flavin”), previously shown to be an SOLsubstituted riboflavin derivative containing a tertiary nitrogen homoconjugated to the flavin nucleus, was subjected to further hydrolysis and to reduction under acid conditions. Both conditions resulted in the liberation of 1 mole of histidine per mole of flavin. This proves histidine to be the covalent link b...

Peptides from complex II active in reconstitution of succinate-ubiquinone reductase.

A preparation has been made from Complex I1 of beef heart mitochondria which contains in purified form two peptides, designated CItw3 and Ctt-4, with molecular weights of 13,500 and 7,000, respectively. Recombination of soluble succinate dehydrogenase with the peptides elicits ubiquinone reductase activity and, with Complex 111, antimycin-sensitive cytochrome c reductase activity, while the “lo...