The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase

被引:84
作者
Toledo-Cuevas, M
Barquera, B
Gennis, RB
Wikström, M
García-Horsman, JA
机构
[1] Univ Helsinki, Dept Med Chem, Inst Biomed, Helsinki Bioenerget Grp, FIN-00014 Helsinki, Finland
[2] Univ Nacl Autonoma Mexico, Inst Fisiol Celular, Dept Bioquim, Mexico City 04510, DF, Mexico
[3] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1998年 / 1365卷 / 03期
关键词
cytochrome oxidase; cytochrome cbb(3); proton pumping; ccoNOQP operon; respiratory system; (Rhodobacter sphaeroides);
D O I
10.1016/S0005-2728(98)00095-4
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
Rhodobacter sphaeroides expresses a bb(3)-type quinol oxidase, and two cytochrome c oxidases, cytochrome aa(3) and cytochrome cbb(3). We report here the characterization of the genes encoding this latter oxidase. The ccoNOQP gene cluster of R. sphaeroides contains four open reading frames with high similarity to all ccoNOQP/fixNOQP gene clusters reported so far. CcoN has the six highly conserved histidines proposed to be involved in binding the low spin heme, and the binuclear center metals. ccoO and ccoP code for membrane bound mono- and diheme cytochromes c. ccoQ codes for a small hydrophobic protein of unknown function. Upstream from the cluster there is a conserved Fnr/FixK-like box which may regulate its expression. Analysis of a R. sphaeroides mutant in which the ccoNOQP gene cluster was inactivated confirms that this cluster encodes the cbb(3)-type oxidase previously purified. Analysis of proton translocation in several strains shows that cytochrome cbb(3) is a proton pump. We also conclude that cytochromes cbb(3) and aa(3) are the only cytochrome c oxidases in the respiratory chain of R sphaeroides. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:421 / 434
页数:14
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