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Please use this identifier to cite or link to this item: http://dspace.utalca.cl/handle/1950/10185

Title: On the mechanism underlying tellurite reduction by Aeromonas caviae ST dihydrolipoamide dehydrogenase
Authors: Arenas, FA..
Leal, CA.
Pinto, CA.
Arenas-Salinas, MA.
Morales, WA.
Cornejo, FA.
Diaz-Vasquez, WA.
Vasquez, CC.
Keywords: Tellurite
LpdA
Aeromonas caviae
Tellurite reduction
Dihydrolipoamide dehydrogenase
Issue Date: Jul-2014
Publisher: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Citation: BIOCHIMIE Volumen: 102C Páginas: 174-182
Abstract: The dihydrolipoamide dehydrogenase (LpdA) from the tellurite-resistant bacterium Aeromonas caviae ST reduces tellurite to elemental tellurium. To characterize this NADH-dependent activity, the A. caviae lpdA gene was subjected to site-directed mutagenesis and genes containing C45A, H322Y and E3541( substitutions were individually transformed into Escherichia coli Delta lpd. Cells expressing the modified genes exhibited decreased pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and TR activity regarding that observed with the wild type A. caviae lpdA gene. In addition, cells expressing the altered lpdA genes showed increased oxidative stress levels and tellurite sensitivity than those carrying the wild type counterpart.
Description: Univ Talca, Ctr Bioinformat & Simulac Mol, Talca, Chile. Morales, WA (Morales, W. A.)
URI: http://dspace.utalca.cl/handle/1950/10185
ISSN: 1638-6183
Appears in Collections:Artículos en publicaciones ISI - Universidad de Talca

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