Asymmetrical Evolution of Cytochrome bd Subunits
نویسندگان
چکیده
منابع مشابه
Molecular Evolution of Cytochrome bd Oxidases across Proteobacterial Genomes
This work is aimed to resolve the complex molecular evolution of cytochrome bd ubiquinol oxidase, a nearly ubiquitous bacterial enzyme that is involved in redox balance and bioenergetics. Previous studies have created an unclear picture of bd oxidases phylogenesis without considering the existence of diverse types of bd oxidases. Integrated approaches of genomic and protein analysis focused on ...
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Vertebrate mitochondrial cytochrome c oxidase (COX) possesses 10 nuclear-encoded subunits. Six subunits have paralogs in mammals, but the origins and distribution of isoforms among vertebrates have not been analyzed. We used Bayesian phylogenetic analysis to interpret the origins of each subunit, inferring the roles of gene and genome duplications. The paralogous ancestries of five genes were i...
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Cytochrome bd is a prokaryotic terminal oxidase that catalyses the electrogenic reduction of oxygen to water using ubiquinol as electron donor. Cytochrome bd is a tri-haem integral membrane enzyme carrying a low-spin haem b558, and two high-spin haems: b595 and d. Here we show that besides its oxidase activity, cytochrome bd from Escherichia coli is a genuine quinol peroxidase (QPO) that reduce...
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Department of Biochemical Sciences and Istituto Pasteur, Fondazione Cenci Bolognetti, Sapienza University of Rome, Rome, Italya; Belozersky Institute of PhysicoChemical Biology, Lomonosov Moscow State University, Leninskie Gory, Moscow, Russian Federationb; Institute for Oriental and Classical Studies, Russian State University for the Humanities, Moscow, Russian Federationc; CNR Institute of Mo...
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In the course of an infection, Salmonella enterica occupies diverse anatomical sites with various concentrations of oxygen (O2) and nitric oxide (NO). These diatomic gases compete for binding to catalytic metal groups of quinol oxidases. Enterobacteriaceae express two evolutionarily distinct classes of quinol oxidases that differ in affinity for O2 and NO as well as stoichiometry of H+ transloc...
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ژورنال
عنوان ژورنال: Journal of Molecular Evolution
سال: 2006
ISSN: 0022-2844,1432-1432
DOI: 10.1007/s00239-005-0005-7