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A cytochrome ba3 functions as a quinol oxidase in Paracoccus denitrificans. Purification, cloning, and sequence comparison.

Authors :
Richter OM
Tao JS
Turba A
Ludwig B
Source :
The Journal of biological chemistry [J Biol Chem] 1994 Sep 16; Vol. 269 (37), pp. 23079-86.
Publication Year :
1994

Abstract

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 ba3. 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.

Details

Language :
English
ISSN :
0021-9258
Volume :
269
Issue :
37
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
8083210