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- W3037996860 abstract "ABSTRACT Microbial reduction of selenite [Se(IV)] and tellurite [Te(IV)] to Se(0) and Te(0) can function as a detoxification mechanism and serve in energy conservation. In this study, Bacillus sp. Y3 was isolated and demonstrated to have an ability of simultaneous reduction of Se(IV) and Te(IV) during aerobic cultivation, with reduction efficiencies of 100% and 90%, respectively. Proteomics analysis revealed that the putative thioredoxin disulfide reductase (TrxR) and sulfate and energy metabolic pathway proteins were significantly upregulated after the addition of Se(IV) and Te(IV). qRT-PCR also showed an increased trxR transcription level in the presence of Se(IV) and Te(IV). Compared with a wild-type Escherichia coli strain, the TrxR-overexpressed E. coli strain showed higher Se(IV) and Te(IV) resistance levels and reduction efficiencies. Additionally, the TrxR showed in vitro Se(IV) and Te(IV) reduction activities when NADPH or NADH were present. When NADPH was used as the electron donor, the optimum conditions for enzyme activities were pH 8.0 and 37°C. The Km values of Te(IV) and Se(IV) were 16.31 and 2.91 mM, and the Vmax values of Te(IV) and Se(IV) were 12.23 and 11.20 µM min−1 mg−1, respectively. The discovery of the new reductive enzyme TrxR enriches the repertoire of the bacterial Se(IV) and Te(IV) resistance and reduction mechanisms. Bacillus sp. Y3 can efficiently reduce Se(IV) and Te(IV) simultaneously. Strain Y3 provides potential applications for selenite and tellurite bioremediation. The TrxR enzyme shows high catalytic activity for reducing Se(IV) and Te(IV). The discovery of TrxR enriches the bacterial Se(IV) and Te(IV) reduction mechanisms." @default.
- W3037996860 created "2020-07-02" @default.
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- W3037996860 date "2020-06-26" @default.
- W3037996860 modified "2023-10-15" @default.
- W3037996860 title "NAD(P)H-dependent thioredoxin-disulfide reductase TrxR is essential for tellurite and selenite reduction and resistance in Bacillus sp. Y3" @default.
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- W3037996860 doi "https://doi.org/10.1093/femsec/fiaa126" @default.
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