The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli
Ehj. Gordon et al., The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli, BIOC BIOP R, 281(3), 2001, pp. 788-794
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Cytochrome cd(1) nitrite reductase from Paracoccus pantotrophus is a dimer;
within each monomer there is a largely alpha-helical domain that contains
the c-type cytochrome centre. The structure of this domain changes signific
antly upon reduction of the heme iron, for which the ligands change from Hi
s17/ His69 to Met106/His69. Overproduction, using an improved Escherichia c
oli expression system, of this c-type cytochrome domain as an independent m
onomer is reported here. The properties of the independent domain are compa
red with those when it is part of dimeric hole or semi-ape cytochrome cd(1)
. (C) 2001 Academic Press.