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Journal articles

Arsenite oxidase, an ancient bioenergetic enzyme.

Abstract : 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 beta-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.
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Contributor : Gilberte Niedergang Connect in order to contact the contributor
Submitted on : Tuesday, November 14, 2006 - 11:45:48 AM
Last modification on : Friday, January 21, 2022 - 3:29:19 AM

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Evelyne Lebrun, Myriam Brugna, Frauke Baymann, Daniel Muller, Didier Lièvremont, et al.. Arsenite oxidase, an ancient bioenergetic enzyme.. Mol Biol Evol, 2003, 20 (5), pp.686-93. ⟨10.1093/molbev/msg071⟩. ⟨hal-00113712⟩



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