Mammalian dihydroorotate – ubiquinone reductase complex. II. Correlation with cytochrome oxidase, mode of linkage with the cytochrome chain, and general properties
1969 ◽
Vol 47
(7)
◽
pp. 725-734
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Keyword(s):
Evidence is presented showing that a dihydroorotate-oxidizing system sediments with mitochondrial enzymes of beef liver in a sucrose gradient. Spectrophotometric experiments now indicate that dihydroorotate is as effective as succinate in reducing the cytochrome b content of whole and sonically disrupted mitochondria. The pyrimidine precursor also reduces the entire cytochrome chain under anaerobic conditions. Additional characterization of the dihydroorotate – ubiquinone reductase complex was carried out with regard to pH and temperature stability, and optima, metal inhibition, and behavior in gel filtration chromatography.
1950 ◽
Vol 183
(1)
◽
pp. 89-103
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2008 ◽
Vol 4
(5)
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Keyword(s):
1974 ◽
Vol 31
(01)
◽
pp. 072-085
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1981 ◽
Vol 45
(01)
◽
pp. 060-064
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1984 ◽
Vol 51
(01)
◽
pp. 016-021
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1982 ◽
Vol 47
(03)
◽
pp. 197-202
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Keyword(s):