EXPRESSION OF THE ESCHERICHIA-COLI CYO OPERON IN PARACOCCUS-DENITRIFICANS RESULTS IN A FULLY ACTIVE QUINOL OXIDASE OF UNEXPECTED HEME COMPOSITION

Authors
SCHROTER T WINTERSTEIN C LUDWIG B RICHTER OMH
Citation
T. Schroter et al., EXPRESSION OF THE ESCHERICHIA-COLI CYO OPERON IN PARACOCCUS-DENITRIFICANS RESULTS IN A FULLY ACTIVE QUINOL OXIDASE OF UNEXPECTED HEME COMPOSITION, FEBS letters, 432(3), 1998, pp. 109-112
Citations number
27
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
432
Issue
3
Year of publication
1998
Pages
109 - 112
Database
ISI
SICI code
0014-5793(1998)432:3<109:EOTECO>2.0.ZU;2-X
Abstract
The cyo operon coding for the membrane-bound bo(3)-type quinol oxidase of Escherichia coli has been expressed in a Paracoccus denitrificans strain deleted in its endogenous ba(3) quinol oxidase, Using the P, de nitrificans qox promoter, the His tagged protein complex is synthesize d to a level comparable to that in E. coli and the enzyme purified in a single step on a metal-chelatiug column. Whereas the activity of the isolated complex matches that of the oxidase purified directly from E . coli, the heterologously expressed oxidase does not show the charact eristic heme composition but now carries heme a in its binuclear site. (C) 1998 Federation of European Biochemical Societies.