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- W2067044687 abstract "Oxidation of the pyrimidine precursor, dihydroorotic acid, by Neurospora mitochondria is linked to the reduction of oxygen through components of the respiratory chain. Respiratory inhibitors piericidin A, antimycin A, and o-phenanthroline inhibit the oxidation of dihydroorotate in whole mitochondria but not after the enzyme is solubilized with butanol and Triton X-100. A naturally occurring inhibitor of the biosynthetic reaction, which is extractable with organic solvents, is present in mitochondrial preparations but is removed during purification. The solubilized enzyme is unstable in the absence of dihydroorotate. After 200-fold further purification, dihydroorotate-quinone reductase is active with quinone electron acceptors such as ubiquinones, benzoquinone, and menadione but not with ferricyanide or cytochrome c. No direct transfer of reducing equivalents to single electron acceptors or molecular oxygen has been demonstrated. The purified enzyme preparation contains a mixture of proteins in the molecular weight range of 150,000–300,000 as determined by gel filtration on Sephadex G-200. Protein-bound FMN was identified as a cofactor present in the preparation which lacked iron, labile sulfide, and FAD." @default.
- W2067044687 created "2016-06-24" @default.
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- W2067044687 date "1971-09-01" @default.
- W2067044687 modified "2023-10-17" @default.
- W2067044687 title "Dihydroorotate-quinone reductase of neurospora crassa mitochondria" @default.
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- W2067044687 doi "https://doi.org/10.1016/s0003-9861(71)80063-2" @default.
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