Malarial dihydroorotate dehydrogenase mediates superoxide radical production.

Abstract

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.

• Authors: J Krungkrai
• Journal: Biochemistry international (Biochem Int) Vol. 24 Issue 5 Pg. 833-9 (Jul 1991) ISSN: 0158-5231 [Print] Australia
• PMID: 1663740 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Cytochrome c Group
• Superoxides
• 4,5-dihydroorotic acid
• Nitroblue Tetrazolium
• Orotic Acid
• 2,6-Dichloroindophenol
• Superoxide Dismutase
• Dihydroorotate Oxidase

Topics

• 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)