Genetic identification of the selenate reductase in <i>Enterobacter cloacae</i> SLD1a-1

Selenium pollution poses risks to ecosystems and human health, largely due to the mobility and toxicity of selenate, a common form found in soil and water. Diverse bacterial species are able to convert soluble selenate into insoluble elemental selenium, but the genes and enzymes that underpin this process are not fully understood. In this study, we identified a gene in <i>Enterobacter cloacae</i> SLD1a-1 that enables the bacterium to catalyze selenate reduction. We showed that this gene produces a functional enzyme even when it is transferred into a different species, <i>Escherichia coli</i>. Protein structure modeling revealed features of the enzyme that help it recognize and reduce selenate. This information advances our understanding of how selenium is enzymatically cycled in the environment.

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Publication Details

Journal
Applied and Environmental Microbiology
Published
2025-11-26
DOI
https://doi.org/10.1128/aem.01796-25
Primary Topic
Selenium in Biological Systems
Type
article
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article

Genetic identification of the selenate reductase in Enterobacter cloacae SLD1a-1

Vikas Nanda, Gerben J. Zylstra, Dylan Klein, Jonathan Phan et al.
Applied and Environmental Microbiology
Selenium in Biological Systems
article

Genetic identification of the selenate reductase in Enterobacter cloacae SLD1a-1

Vikas Nanda, Gerben J. Zylstra, Dylan Klein, Jonathan Phan, Nathan Yee
article en

Abstract

Selenium pollution poses risks to ecosystems and human health, largely due to the mobility and toxicity of selenate, a common form found in soil and water. Diverse bacterial species are able to convert soluble selenate into insoluble elemental selenium, but the genes and enzymes that underpin this process are not fully understood. In this study, we identified a gene in <i>Enterobacter cloacae</i> SLD1a-1 that enables the bacterium to catalyze selenate reduction. We showed that this gene produces a functional enzyme even when it is transferred into a different species, <i>Escherichia coli</i>. Protein structure modeling revealed features of the enzyme that help it recognize and reduce selenate. This information advances our understanding of how selenium is enzymatically cycled in the environment.

Applied and Environmental MicrobiologyVol. 91(12)
Rutgers, The State University of New Jersey (US), Planetary Science Institute (US), Johnson University (US), Rutgers Sexual and Reproductive Health and Rights (NL)
Openalex Percentile: Top 56%
Selenium in Biological Systems
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