Cytochrome c1 from Paracoccus denitrificans
Open Access
- 1 December 1983
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 137 (3) , 597-602
- https://doi.org/10.1111/j.1432-1033.1983.tb07867.x
Abstract
Cytochrome c1 was purified from the bacterium Paracoccus denitrificans. It is an acidic, hydrophobic polypeptide with an apparent molecular weight of around 65000 and a single, covalently attached heme; it crossreacts immunologically with cytochrome c1 from yeast mitochondria. The amino acid sequence of the tryptic heme peptide of the bacterial cytochrome c1 shows extensive homology to the corresponding region of beef heart cytochrome c1 [Wakabayashi, S. et al. (1982) J. Biol. Chem. 257, 9335–9344]. Positive evidence for a stable association of the Paracoccus cytochrome c1 with other polypeptides and b-type heme components (‘bc1 -complex’) has not yet been obtained.This publication has 28 references indexed in Scilit:
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