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A cytochrome ba3 functions as a quinol oxidase in Paracoccus denitrificans. Purification, cloning, and sequence comparison.
- 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.
- Subjects :
- Amino Acid Sequence
Base Sequence
Chromatography, Ion Exchange
Cloning, Molecular
Copper metabolism
Cross Reactions
Cytochrome b Group genetics
Cytochrome b Group immunology
Cytochrome b Group isolation & purification
DNA, Bacterial
Electron Transport Complex IV genetics
Electron Transport Complex IV immunology
Electron Transport Complex IV isolation & purification
Electrophoresis, Polyacrylamide Gel
Heme metabolism
Molecular Sequence Data
Peptide Mapping
Sequence Homology, Amino Acid
Cytochrome b Group metabolism
Electron Transport Complex IV metabolism
Oxidoreductases metabolism
Paracoccus denitrificans enzymology
Subjects
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