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MBE Advance Access originally published online on April 2, 2003
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Mol. Biol. Evol. 20(5):686-693. 2003
DOI: 10.1093/molbev/msg071
© 2003 by the Society for Molecular Biology and Evolution. ISSN: 0737-4038

Arsenite Oxidase, an Ancient Bioenergetic Enzyme

Evelyne Lebrun*, Myriam Brugna*,1, Frauke Baymann*, Daniel Muller{dagger}, Didier Lièvremont{dagger}, Marie-Claire Lett{dagger} and Wolfgang Nitschke*,

* Laboratoire de Bioénergétique et Ingénierie des Protéines, Institut de Biologie Structurale et Microbiologie, Marseille Cedex, France
{dagger} Laboratoire de Dynamique, Evolution et Expression des Génomes de Micro-Organismes, Université Louis-Pasteur, Strasbourg Cedex, France

Operons coding for the enzyme arsenite oxidase have been detected in the genomes from Archaea and Bacteria by Blast searches using the amino acid sequences of the respective enzyme characterized in two different ß-proteobacteria as templates. Sequence analyses show that in all these species, arsenite oxidase is transported over the cytoplasmic membrane via the tat system and most probably remains membrane attached by an N-terminal transmembrane helix of the Rieske subunit. The biochemical and biophysical data obtained for arsenite oxidase in the green filamentous bacterium Chloroflexus aurantiacus allow a structural model of the enzyme's membrane association to be proposed. Phylogenies for the two constituent subunits (i.e., the molybdopterin-containing and the Rieske subunit) of the heterodimeric enzyme and their respective homologs in DMSO-reductase, formate dehydrogenase, nitrate reductase, and the Rieske/cytb complexes were calculated from multiple sequence alignments. The obtained phylogenetic trees indicate an early origin of arsenite oxidase before the divergence of Archaea and Bacteria. Evolutionary implications of these phylogenies are discussed.

Key Words: arsenite • bioenergetics • evolution • phylogeny • Rieske protein • molybdopterin protein


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