title: Isolation of succinate dehydrogenase from Desulfobulbus elongatus, a propionate oxidizing, sulfate reducing bacterium.
abstract: Succinate dehydrogenase was purified from the particulate fraction of Desulfobulbus. The enzyme catalyzed both fumarate reduction and succinate oxidation but the rate of fumarate reduction was 8-times less than that of succinate oxidation. Quantitative analysis showed the presence of 1 mol of covalently bound flavin and 1 mol of cytochrome b per mol of succinate dehydrogenase. The enzyme contained three subunits with molecular mass 68.5, 27.5 and 22 kDa. EPR spectroscopy indicated the presence of at least two iron sulfur clusters. 2-Heptyl-4-hydroxy-quinoline-N-oxide inhibited the electron-transfer between succinate dehydrogenase and a high redox potential cytochrome c3 from Desulfobulbus elongatus.
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D005650:Fumarates / Q000378:metabolism; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism; D013379:Substrate Specificity; D013385:Succinate Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D013386:Succinates / Q000378:metabolism; D019802:Succinic Acid
chemical_list: D001426:Bacterial Proteins; D005650:Fumarates; D008565:Membrane Proteins; D013386:Succinates; C032005:fumaric acid; D019802:Succinic Acid; D013385:Succinate Dehydrogenase