A CYTOCHROME BA(3) FUNCTIONS AS A QUINOL OXIDASE IN PARACOCCUS-DENITRIFICANS - PURIFICATION, CLONING, AND SEQUENCE COMPARISON

被引：0
|
作者：
RICHTER, OMH [1 ]
TAO, JS [1 ]
TURBA, A [1 ]
LUDWIG, B [1 ]
机构：
[1] UNIV FRANKFURT,BIOZENTRUM N200,INST BIOCHEM,DEPT MOLEC GENET,D-60439 FRANKFURT,GERMANY
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 1994年 / 269卷 / 37期
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D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A quinol oxidase has been purified from the cytoplasmic membrane of Paracoccus denitrificans; its heme composition and CO binding properties identify it as a cytochrome ba(3). On SDS gels, the purified enzyme complex is separated into five polypeptides. Using partial peptide sequence information for subunit II, the gene locus has been cloned and sequenced. In a typical operon pattern, four genes were identified: qoxA, -B, -C, and -D, coding for subunits II, I, III, and IV. DNA-derived amino acid sequence comparisons reveal extensive similarities to other members of the terminal oxidase superfamily.
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页码：23079 / 23086
页数：8
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