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7845144 
Journal Article 
Malarial dihydroorotate dehydrogenase mediates superoxide radical production 
Krungkrai, J 
1991 
Yes 
Biochemistry International
ISSN: 0158-5231 
24 
5 
833-839 
English 
1663740 
Dihydroorotate dehydrogenase purified from mitochondria of Plasmodium berghei, a rodent malaria parasite, mediates production of superoxide radical during oxidation of dihydroorotate to orotate. Reduction of dichlorophenolindophenol or cytochrome c or nitroblue tetrazolium was significantly inhibited by superoxide dismutase or theonyltrifluoroacetone, a specific iron chelator of the enzyme. These results, together with the recent evidence of manganese-superoxide dismutase activity in malarial mitochondria [Ranz, A., and Meshnick, S.R. (1989) Exp. Parasitol. 69, 125-128], suggest that the production of superoxide radical may occur in vivo. 
2,6-Dichloroindophenol/metabolism; Animals; Cytochrome c Group/metabolism; Dihydroorotate Oxidase/isolation & purification/metabolism; Electrophoresis, Polyacrylamide Gel; Mitochondria/metabolism; Nitroblue Tetrazolium/metabolism; Orotic Acid/analogs & derivatives/metabolism; Oxidation-Reduction; Plasmodium berghei/enzymology; Plasmodium falciparum/enzymology; Superoxide Dismutase/pharmacology; Superoxides/metabolism