AUTHOR=Arenas-Salinas Mauricio , Vargas-Pérez Joaquín I. , Morales Wladimir , Pinto Camilo , Muñoz-Díaz Pablo , Cornejo Fabián A. , Pugin Benoit , Sandoval Juan M. , Díaz-Vásquez Waldo A. , Muñoz-Villagrán Claudia , Rodríguez-Rojas Fernanda , Morales Eduardo H. , Vásquez Claudio C. , Arenas Felipe A. TITLE=Flavoprotein-Mediated Tellurite Reduction: Structural Basis and Applications to the Synthesis of Tellurium-Containing Nanostructures JOURNAL=Frontiers in Microbiology VOLUME=7 YEAR=2016 URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2016.01160 DOI=10.3389/fmicb.2016.01160 ISSN=1664-302X ABSTRACT=
The tellurium oxyanion tellurite (TeO32-) is extremely harmful for most organisms. It has been suggested that a potential bacterial tellurite resistance mechanism would consist of an enzymatic, NAD(P)H-dependent, reduction to the less toxic form elemental tellurium (Te0). To date, a number of enzymes such as catalase, type II NADH dehydrogenase and terminal oxidases from the electron transport chain, nitrate reductases, and dihydrolipoamide dehydrogenase (E3), among others, have been shown to display tellurite-reducing activity. This activity is generically referred to as tellurite reductase (TR). Bioinformatic data resting on some of the abovementioned enzymes enabled the identification of common structures involved in tellurite reduction including vicinal catalytic cysteine residues and the FAD/NAD(P)+-binding domain, which is characteristic of some flavoproteins. Along this line, thioredoxin reductase (TrxB), alkyl hydroperoxide reductase (AhpF), glutathione reductase (GorA), mercuric reductase (MerA), NADH: flavorubredoxin reductase (NorW), dihydrolipoamide dehydrogenase, and the putative oxidoreductase YkgC from