The cbb3 oxidases are an ancient innovation of the domain bacteria

被引：71

作者：

Ducluzeau, Anne-Lise ^{[1
]}

Ouchane, Soufian ^{[2
]}

Nitschke, Wolfgang ^{[1
]}

机构：

[1] CNRS, Inst Biol Struct & Microbiol, Lab Bioenerget & Ingn Prot, UPR 9036, Marseille, France

[2] Univ Paris 06, Ctr Genet Mol, CNRS, UPR 2167, Gif Sur Yvette, France

来源：

MOLECULAR BIOLOGY AND EVOLUTION | 2008年 / 25卷 / 06期

关键词：

D O I：

10.1093/molbev/msn062

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：

A survey of genomes for the presence of gene clusters related to cbb(3) oxidases detected bona fide members of the family in almost all phyla of the domain Bacteria. No archaeal representatives were found. The subunit composition was seen to vary substantially between clades observed on the phylogenetic tree of the catalytic subunit CcoN. The protein diade formed by CcoN and the monoheme cytochrome CcoO appears to constitute the functionally essential "core" of the enzyme conserved in all sampled cbb(3) gene clusters. The topology of the phylogenetic tree contradicts the scenario of a recent origin of cbb(3) oxidases and substantiates the status of this family as a phylogenetic entity on the same level as the other subgroups of the heme-copper superfamily (including nitric oxide reductase). This finding resuscitates and exacerbates the conundrum of the evolutionary origin of heme-copper oxidases.

引用

页码：1158 / 1166

页数：9

共 48 条

[1] The structure of Acidithiobacillus ferrooxidans c4-cytochrome:: A model for complex-induced electron transfer tuning [J].