title: Nitrate reductase from Spinacea oleracea. FAD and the reactivation of the enzyme treated with p-Hydroxymercuribenzoate.
abstract: Spinach nitrate reductase complex previously inactivated by treatment with mercurials p-hydroxymercuribenzoate or p-hydroxymercuriphenyl sulphonate can be reactivated by incubation with dithioerythritol. The reactivation of NADH-diaphorase seems to be FAD-dependent, whereas that of FNH2-nitrate reductase is not. The requirement of FAD for NADH-inactivation of nitrate reductase treated with p-hydroxymercuribenzoate disappears after treatment with dithioerythritol.
mesh_terms: D008058:Dihydrolipoamide Dehydrogenase / Q000032:analysis; D004793:Enzyme Reactivators; D005182:Flavin-Adenine Dinucleotide / Q000032:analysis*; D008626:Mercuribenzoates / Q000494:pharmacology; D009565:Nitrate Reductases / Q000032:analysis*; D014675:Vegetables / Q000032:analysis*
chemical_list: D004793:Enzyme Reactivators; D008626:Mercuribenzoates; D005182:Flavin-Adenine Dinucleotide; D009565:Nitrate Reductases; D008058:Dihydrolipoamide Dehydrogenase