Bogaart A M, Bernini L F
Biochem Genet. 1981 Oct;19(9-10):929-46. doi: 10.1007/BF00504258.
Sulfite oxidase (sulfite: ferricytochrome c oxidoreductase; EC 1.8.2.1) has been detected in Drosophila melanogaster and some of its properties have been studied. In most respects this enzyme resembles the mammalian sulfite oxidases except for its molecular weight (148,000), which is somewhat higher than that of rat sulfite oxidase (116,000). Cytochrome c, potassium-ferricyanide, and oxygen can serve as electron acceptors in the oxidation of sulfite by the enzyme. Although definite evidence can be obtained only through the analysis of the pure enzyme, experiments involving tungstate feeding suggest that Drosophila sulfite oxidase is most probably a molybdoenzyme. Extracts of mal flies show normal levels of sulfite oxidase, whereas lxd flies have only 5-10% of the activity of wild type, and in cin flies the enzyme is apparently absent. While it is possible that the lxd and cin mutations are at some level responsible for the defective synthesis of a molybdenum-containing cofactor (supposed to be present in most molybdoenzymes), the evidence accumulated so far by several authors and the results of the present investigation argue against the involvement of a Mo cofactor in the multiple enzyme deficiencies observed in mal flies.
在黑腹果蝇中已检测到亚硫酸盐氧化酶（亚硫酸盐：铁细胞色素c氧化还原酶；EC 1.8.2.1），并对其一些特性进行了研究。在大多数方面，这种酶类似于哺乳动物的亚硫酸盐氧化酶，只是其分子量（148,000）略高于大鼠亚硫酸盐氧化酶（116,000）。细胞色素c、铁氰化钾和氧气可作为该酶氧化亚硫酸盐时的电子受体。虽然只有通过对纯酶的分析才能获得确切证据，但涉及钨酸盐喂养的实验表明，果蝇亚硫酸盐氧化酶很可能是一种钼酶。雄蝇提取物中亚硫酸盐氧化酶水平正常，而lxd果蝇的活性仅为野生型的5-10%，在cin果蝇中显然不存在该酶。虽然lxd和cin突变在某种程度上可能导致含钼辅因子（大多数钼酶中应该存在）合成缺陷，但几位作者目前积累的证据以及本研究结果表明，钼辅因子与在雄蝇中观察到的多种酶缺陷无关。
