ArticleFEMS microbiology ecology2020
Identification of a TeO32- reductase/mycothione reductase from Rhodococcus erythropolis PR4.
Article in FEMS microbiology ecology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers, 1 of them a synthesis that pooled it.
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Who cites it
7 citing papers in PubMed, 1 synthesis or guideline pooled it, 11 citations in OpenAlex.
- Microbial mechanisms to transform the super-trace element tellurium: a systematic review and discussion of nanoparticulate phases.World journal of microbiology & biotechnology · 2023Pooled it
- Cloneable contrast across all biological length scales.Journal of structural biology · 2026Article
- Molecular tags for electron cryo-tomography.Emerging topics in life sciences · 2025Review
- Exploring the Potential of Glutathione Reductase Overexpression to Improve Tellurium Nanoparticle Production inInternational journal of molecular sciences · 2025Article
- The crystal structure of mycothiol disulfide reductase (Mtr) provides mechanistic insight into the specific low-molecular-weight thiol reductase activity of Actinobacteria.Acta crystallographica. Section D, Structural biology · 2024Article
- Cloneable inorganic nanoparticles.Chemical communications (Cambridge, England) · 2023Review
- Novel biosynthesis of tellurium nanoparticles and investigation of their activity against common pathogenic bacteria.Journal of Taibah University Medical Sciences · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A Rhodococcus erythropolis bacterium that tolerates normally lethal concentrations of Fe(II), Cu(II), AsO32-, SeO32-, TeO32-, Cd(II) and Zn(II) was identified from an environmental isolate. In characterizing the molecular basis for metal tolerance, a mycothione reductase (Mtr) with remarkable selectivity for TeO32- reduction over SeO32- was identified. In equimolar concentrations of TeO32- and SeO32-, the enzymatic product contains a 7-fold excess of Te. This selectivity is remarkable because the standard reduction potential of SeO32- is 0.20 V more favorable for reduction than TeO32. Selectivity of the enzyme for TeO32- decreases with increasing assay pH. Homology modeling of the enzyme identifies four aromatic residues near the active site, including two histidine residues, that are not present in a related SeO32- preferring reductase. On the basis of more favorable π-interactions for Te than for Se and the pH dependence of the selectivity, the Te-selectivity is attributed in part to these aromatic residues. The resulting Te0 enzymatic product resembles Te nanowires.
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Registered trials
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