ArticleThe Journal of biological chemistry2011
Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from Pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 32 citations in OpenAlex.
- Structural and functional characterization of dihydrodiol dehydrogenase PahB recognizing high-molecular-weight PAH substrates.Applied and environmental microbiology · 2026Article
- A Unique Insertion Loop Facilitates Tight NADInternational journal of molecular sciences · 2026Article
- Identification, functional characterization, and structural analysis of an atypical l-threonate 3-dehydrogenase.The Journal of biological chemistry · 2026Article
- Structure, kinetics, and mechanism of Pseudomonas putida sulfoquinovose dehydrogenase, the first enzyme in the sulfoglycolytic Entner-Doudoroff pathway.The Biochemical journal · 2025Article
- Purification and characterization of a Rieske oxygenase and its NADH-regenerating partner proteins.Methods in enzymology · 2024Article
- Structural Insights into Dihydroxylation of Terephthalate, a Product of Polyethylene Terephthalate Degradation.Journal of bacteriology · 2022Article
- A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Engineering Burkholderia xenovorans LB400 BphA through Site-Directed Mutagenesis at Position 283.Applied and environmental microbiology · 2020Article
- Whole Genome Sequencing and Comparative Genomics Analyses ofFrontiers in microbiology · 2019Article
- Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.Scientific reports · 2017Article
- Structural Basis of the Enhanced Pollutant-Degrading Capabilities of an Engineered Biphenyl Dioxygenase.Journal of bacteriology · 2016Article
- Article
- Dynamic characterization and substrate binding of cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase-an enzyme used in bioremediation.Journal of molecular modeling · 2014Article
- Pandoraea sp. RB-44, a novel quorum sensing soil bacterium.Sensors (Basel, Switzerland) · 2013Article
- Has the bacterial biphenyl catabolic pathway evolved primarily to degrade biphenyl? The diphenylmethane case.Journal of bacteriology · 2013Article
- Article
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6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Biphenyl dehydrogenase, a member of short-chain dehydrogenase/reductase enzymes, catalyzes the second step of the biphenyl/polychlorinated biphenyls catabolic pathway in bacteria. To understand the molecular basis for the broad substrate specificity of Pandoraea pnomenusa strain B-356 biphenyl dehydrogenase (BphB(B-356)), the crystal structures of the apo-enzyme, the binary complex with NAD(+), and the ternary complexes with NAD(+)-2,3-dihydroxybiphenyl and NAD(+)-4,4'-dihydroxybiphenyl were determined at 2.2-, 2.5-, 2.4-, and 2.1-Å resolutions, respectively. A crystal structure representing an intermediate state of the enzyme was also obtained in which the substrate binding loop was ordered as compared with the apo and binary forms but it was displaced significantly with respect to the ternary structures. These five structures reveal that the substrate binding loop is highly mobile and that its conformation changes during ligand binding, starting from a disorganized loop in the apo state to a well organized loop structure in the ligand-bound form. Conformational changes are induced during ligand binding; forming a well defined cavity to accommodate a wide variety of substrates. This explains the biochemical data that shows BphB(B-356) converts the dihydrodiol metabolites of 3,3'-dichlorobiphenyl, 2,4,4'-trichlorobiphenyl, and 2,6-dichlorobiphenyl to their respective dihydroxy metabolites. For the first time, a combination of structural, biochemical, and molecular docking studies of BphB(B-356) elucidate the unique ability of the enzyme to transform the cis-dihydrodiols of double meta-, para-, and ortho-substituted chlorobiphenyls.
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