flavin-adenine-dinucleotide and malonic-acid

The Saccharomyces cerevisiae succinate-ubiquinone reductase or succinate dehydrogenase (SDH) is a tetramer of non-equivalent subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. In most organisms, SDH contains one or two endogenous b-type hemes. However, it is widely believed that the yeast SDH does not contain heme. In this report, we demonstrate the presence of a stoichiometric amount of cytochrome b562 in the yeast SDH. The cytochrome is detected as a peak present in fumarate-oxidized, dithionite-reduced mitochondria. The peak is centered at 562 nm and is present at a heme:covalent FAD molar ratio of 0.92+/-0.11. The cytochrome is not detectable in mitochondria isolated from SDH3 and SDH4 deletion strains. These observations strongly support our conclusion that cytochrome b562 is a component of the yeast SDH.

Topics: Animals; Cytochrome b Group; Dithionite; Electron Transport Complex II; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Fumarates; Fungal Proteins; Gene Deletion; Intracellular Membranes; Lactic Acid; Malonates; Mice; Mitochondria; Multienzyme Complexes; Oxidation-Reduction; Oxidoreductases; Saccharomyces cerevisiae; Spectrum Analysis; Succinate Dehydrogenase