The dihydrolipoamide dehydrogenase of Aeromonas caviae ST exhibits NADH-dependent tellurite reductase activity

Castro, Miguel E.; Molina, Roberto C.; Díaz, Waldo A.; Pîchuantes, Sergio; Vásquez, Claudio C.

doi:10.1016/j.bbrc.2008.07.119

Cited by 54 publications

(61 citation statements)

References 28 publications

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“…GOR seemed the best candidate to reduce tellurite since it belongs to the flavoprotein disulfide reductase (FDR) family, whose members are characterized by the presence of flavin as cofactor. This family also includes dihydrolipoamide dehydrogenase, previously reported as TR in our laboratory (8).…”

Section: Resultsmentioning

confidence: 93%

Glutathione Reductase-Mediated Synthesis of Tellurium-Containing Nanostructures Exhibiting Antibacterial Properties

Pugin

Cornejo

Muñoz-Díaz

et al. 2014

Appl Environ Microbiol

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Tellurium, a metalloid belonging to group 16 of the periodic table, displays very interesting physical and chemical properties and lately has attracted significant attention for its use in nanotechnology. In this context, the use of microorganisms for synthesizing nanostructures emerges as an eco-friendly and exciting approach compared to their chemical synthesis. To generate Tecontaining nanostructures, bacteria enzymatically reduce tellurite to elemental tellurium. In this work, using a classic biochemical approach, we looked for a novel tellurite reductase from the Antarctic bacterium Pseudomonas sp. strain BNF22 and used it to generate tellurium-containing nanostructures. A new tellurite reductase was identified as glutathione reductase, which was subsequently overproduced in Escherichia coli. The characterization of this enzyme showed that it is an NADPH-dependent tellurite reductase, with optimum reducing activity at 30°C and pH 9.0. Finally, the enzyme was able to generate Te-containing nanostructures, about 68 nm in size, which exhibit interesting antibacterial properties against E. coli, with no apparent cytotoxicity against eukaryotic cells.

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Section: Resultsmentioning

confidence: 93%

Glutathione Reductase-Mediated Synthesis of Tellurium-Containing Nanostructures Exhibiting Antibacterial Properties

Pugin

Cornejo

Muñoz-Díaz

et al. 2014

Appl Environ Microbiol

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“…Dihydrolipoamide dehydrogenase has also been implicated in reducing cellular nitric oxide [27], iron [28], and tellurite [29]. Although dihydrolipoamide dehydrogenase is normally an intracellular enzyme [22,25,26] there are reports of cell surface dehydrolipoamide dehydrogenase enzyme activities in Pseudomonas aeruginosa [30],…”

Section: Discussionmentioning

confidence: 99%

Identification of an extracellular bacterial flavoenzyme that can prevent re-polymerisation of lignin fragments

Rahmanpour

King

Bugg

2017

Biochemical and Biophysical Research Communications

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Abstract. A significant problem in the oxidative breakdown of lignin is the tendency of phenolic radical fragments to re-polymerise to form higher molecular weight species. In this paper we identify an extracellular flavin-dependent dehydrolipoamide dehydrogenase from Thermobifida fusca that prevents oxidative dimerization of a dimeric lignin model compound, which could be used as an accessory enzyme for lignin depolymerisation.

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“…More recently, we have shown that overproduction of the Aeromonas caviae ST dihydrolipoil dehydrogenase results in enhanced tellurite resistance in E. coli. This enzyme exhibits NADH-dependent tellurite reductase (TR) activity (Castro et al, 2008(Castro et al, , 2009). The change of two defined amino acid residues at the enzyme active site decreased TR activity (unpublished data).…”

Section: The Enigma Of Tellurite Toxicitymentioning

confidence: 99%

“…In addition to its high resistance to tellurite, this strain exhibited high levels of tellurite reduction, as determined by the darkness of cells exposed to the toxic salt and by tellurite reductase (TR) enzymatic assays performed with cell-free extracts. Interestingly, most of this TR activity was dependent of NADH and tracked to the pyruvate dehydrogenase multienzymatic complex (PDH), specifically to the E3 component encoded by the lpdA gene (Castro et al, 2008(Castro et al, , 2009). …”

Section: Lpdamentioning

confidence: 99%

“…These mutants were chosen based on previous work on the E. coli E3 component indicating that C45 is highly conserved and is involved in the formation of a disulfide bond with C50, required for appropriate protein conformation (Kim et al, 2008). H322 and E354 were changed to Y and K, respectively, because it was previously shown that these mutations affect NADH binding, a substrate required for PDH as well as for TR activity (Castro et al, 2008(Castro et al, , 2009). …”

Section: Lpdamentioning

confidence: 99%

See 1 more Smart Citation

Site-Directed Mutagenesis as a Tool for Unveiling Mechanisms of Bacterial Tellurite Resistance

Pérez-Donoso¹,

Vásquez²

2013

Genetic Manipulation of DNA and Protein - Examples From Current Research

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The dihydrolipoamide dehydrogenase of Aeromonas caviae ST exhibits NADH-dependent tellurite reductase activity

Cited by 54 publications

References 28 publications

Glutathione Reductase-Mediated Synthesis of Tellurium-Containing Nanostructures Exhibiting Antibacterial Properties

Glutathione Reductase-Mediated Synthesis of Tellurium-Containing Nanostructures Exhibiting Antibacterial Properties

Identification of an extracellular bacterial flavoenzyme that can prevent re-polymerisation of lignin fragments

Site-Directed Mutagenesis as a Tool for Unveiling Mechanisms of Bacterial Tellurite Resistance

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