Open AccessThe Paracoccus denitrificans cytochrome aa 3 has a third subunit
Author(s) -
HALTIA Tuomas,
PUUSTINEN Anne,
FINEL Moshe
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb13923.x
Subject(s) - paracoccus denitrificans , cytochrome c oxidase , protein subunit , biochemistry , enzyme , peptide sequence , oxidase test , biology , cytochrome , stereochemistry , microbiology and biotechnology , chemistry , gene
The presence of a third polypeptide subunit in Paracoccus cytochrome c oxidase is demonstrated. This protein (apparent molecular mass 23 kDa) binds dicyclohexylcarbodiimide in membranes of aerobically grown bacteria and in the purified enzyme. The N‐terminal amino‐acid sequence of this dicyclohexylcarbodiimide‐binding protein is identical to the deduced sequence of the COIII gene product [Raitio et al. (1987) EMBO J. 6 , 2825–2833]. We conclude that the aa 3 ‐type oxidase in Paracoccus is composed of at least three subunits, which correspond to the three mitochondrially coded polypeptides in the eukaryotic enzyme.