ArticleProceedings of the National Academy of Sciences of the United States of America2021
A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 14 citations in OpenAlex.
- Structural and mechanistic basis for the heterotetrameric benzaldehyde synthase from petunia.Science advances · 2026Article
- Specific residues and conformational plasticity define the substrate specificity of short-chain dehydrogenases/reductases.The Journal of biological chemistry · 2024Article
- Genome-wide identification and functional characterization of borneol dehydrogenases in Wurfbainia villosa.Planta · 2023Article
- Volatile Organic Compounds fromApplied and environmental microbiology · 2023Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Polychlorinated biphenyls (PCBs) are persistent organic pollutants with severe effects on human health and the biosphere. Plant-based remediation offers many benefits over conventional PCB remediation, but its development has been hampered by our poor understanding of biphenyl metabolism in eukaryotes, among other factors. We report here a major PCB-responsive protein in poplar, a plant model system capable of PCB uptake and translocation. We provide structural and functional evidence that this uncharacterized protein, termed SDR57C, belongs to the heterogeneous short-chain dehydrogenase reductase (SDR) superfamily. Despite sequence divergence, structural modeling hinted at structural and functional similarities between SDR57C and BphB, a central component of the Bph pathway for biphenyl/PCB degradation in aerobic bacteria. By combining gas chromatography/mass spectrometry (GC/MS) profiling with a functional complementation scheme, we found that poplar SDR57C can replace BphB activity in the upper Bph pathway of
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