ArticlePloS one2013
Structural characterization of Pandoraea pnomenusa B-356 biphenyl dioxygenase reveals features of potent polychlorinated biphenyl-degrading enzymes.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Enhanced Biphenyl Degradation byMicroorganisms · 2026Article
- Structure-guided engineering of an aromatic ring-hydroxylating dioxygenase for broad-spectrum phthalate degradation.Journal of bacteriology · 2025Article
- Rieske Oxygenases: Powerful Models for Understanding Nature's Orchestration of Electron Transfer and Oxidative Chemistry.Biochemistry · 2025Review
- Differential effect of monoterpenes and flavonoids on the transcription of aromatic ring-hydroxylating dioxygenase genes inMicrobial genomics · 2025Article
- The α- and β-Subunit Boundary at the Stem of the Mushroom-Like αApplied and environmental microbiology · 2022Article
- Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Insights into Dihydroxylation of Terephthalate, a Product of Polyethylene Terephthalate Degradation.Journal of bacteriology · 2022Article
- Differential proteomic analysis under pesticides stress and normal conditions in Bacillus cereus 2D.PloS one · 2021Article
- Biodegradation of Lignin Monomers Vanillic, p-Coumaric, and Syringic Acid by the Bacterial Strain, Sphingobacterium sp. HY-H.Current microbiology · 2018Article
- Characterization of a di-n-butyl phthalate-degrading bacterial consortium and its application in contaminated soil.Environmental science and pollution research international · 2018Article
- Relationship between the binding free energy and PCBs' migration, persistence, toxicity and bioaccumulation using a combination of the molecular docking method and 3D-QSAR.Chemistry Central journal · 2018Article
- Spatial Patterns of bphA Gene Diversity Reveal Local Adaptation of Microbial Communities to PCB and PAH Contaminants.Microbial ecology · 2016Article
- Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase.Journal of bacteriology · 2016Article
- Investigating the degradation process of kraft lignin by β-proteobacterium, Pandoraea sp. ISTKB.Environmental science and pollution research international · 2015Article
- Metabolism of Doubly para-Substituted Hydroxychlorobiphenyls by Bacterial Biphenyl Dioxygenases.Applied and environmental microbiology · 2015Article
- Article
- Proteomic strategy for the analysis of the polychlorobiphenyl-degrading cyanobacterium Anabaena PD-1 exposed to Aroclor 1254.PloS one · 2014Article
- Biodegradation of endocrine disruptors in solid-liquid two-phase partitioning systems by enrichment cultures.Applied and environmental microbiology · 2013Article
- Has the bacterial biphenyl catabolic pathway evolved primarily to degrade biphenyl? The diphenylmethane case.Journal of bacteriology · 2013Article
- Spectroscopic studies of the mononuclear non-heme Fe(II) enzyme FIH: second-sphere contributions to reactivity.Journal of the American Chemical Society · 2013Article
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Abstract
The oxidative degradation of biphenyl and polychlorinated biphenyls (PCBs) is initiated in Pandoraea pnomenusa B-356 by biphenyl dioxygenase (BPDO(B356)). BPDO(B356), a heterohexameric (αβ)(3) Rieske oxygenase (RO), catalyzes the insertion of dioxygen with stereo- and regioselectivity at the 2,3-carbons of biphenyl, and can transform a broad spectrum of PCB congeners. Here we present the X-ray crystal structures of BPDO(B356) with and without its substrate biphenyl 1.6-Å resolution for both structures. In both cases, the Fe(II) has five ligands in a square pyramidal configuration: H233 Nε2, H239 Nε2, D386 Oδ1 and Oδ2, and a single water molecule. Analysis of the active sites of BPDO(B356) and related ROs revealed structural features that likely contribute to the superior PCB-degrading ability of certain BPDOs. First, the active site cavity readily accommodates biphenyl with minimal conformational rearrangement. Second, M231 was predicted to sterically interfere with binding of some PCBs, and substitution of this residue yielded variants that transform 2,2'-dichlorobiphenyl more effectively. Third, in addition to the volume and shape of the active site, residues at the active site entrance also apparently influence substrate preference. Finally, comparison of the conformation of the active site entrance loop among ROs provides a basis for a structure-based classification consistent with a phylogeny derived from amino acid sequence alignments.
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