Expression of the Escherichia coli cyo operon in Paracoccus denitrificans results in a fully active quinol oxidase of unexpected heme composition

被引:13
作者
Schröter, T [1 ]
Winterstein, C [1 ]
Ludwig, B [1 ]
Richter, OMH [1 ]
机构
[1] Univ Frankfurt, Mol Genet Biozentrum, D-60439 Frankfurt, Germany
关键词
heme-copper terminal oxidase; quinol oxidase; cytochrome ba; heme promiscuity; heterologous expression;
D O I
10.1016/S0014-5793(98)00839-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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, denitrificans qox promoter, the His tagged protein complex is synthesized 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 characteristic heme composition but now carries heme a in its binuclear site. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:109 / 112
页数:4
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