I. Zickermann et al., EXPRESSION STUDIES ON THE BA(3) QUINOL OXIDASE FROM PARACOCCUS-DENITRIFICANS - A BB(3) VARIANT IS ENZYMATICALLY INACTIVE, European journal of biochemistry, 246(3), 1997, pp. 618-624
Expression of the quinol oxidase from Paracoccus denitrificans has bee
n examined using a polyclonal antibody directed against subunit II and
a promoter probe vector carrying the promoter region of the qox opero
n. Under aerobic conditions nitrate and nitrite act as specific induce
rs of the expression. To obtain an enzymatically competent quinol oxid
ase complex, an intact ctaB gene is required, which constitutes part o
f the cta operon coding for the an, cytochrome c oxidase of P. denitri
ficans. Deletion of ctaB leads to a change in heme composition of the
quinol oxidase with heme b replacing the high-spin heme a of the binuc
lear center, causing loss of electron transport activity.