1.3.1.56 Dynamic characterization and substrate binding of cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase - an enzyme used in bioremediation Pandoraea pnomenusa 1.3.1.56 Dynamic characterization and substrate binding of cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase - an enzyme used in bioremediation Pandoraea pnomenusa B-356 1.3.1.56 Insights into the catalytic mechanism of dehydrogenase BphB A quantum mechanics/molecular mechanics study Pandoraea pnomenusa 1.3.1.56 Insights into the catalytic mechanism of dehydrogenase BphB A quantum mechanics/molecular mechanics study Pandoraea pnomenusa B-356 1.3.1.56 Active site residues of cis-2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni strain B-356 Comamonas testosteroni 1.3.1.56 Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from Pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme Comamonas testosteroni 1.3.1.56 Biotransformation of indole by whole cells of recombinant biphenyl dioxygenase and biphenyl-2,3-dihydrodiol-2,3-dehydrogenase Dyella ginsengisoli 1.3.1.56 Biotransformation of natural and synthetic isoflavonoids by two recombinant microbial enzymes Burkholderia sp. 1.3.1.56 Biotransformation of natural and synthetic isoflavonoids by two recombinant microbial enzymes Burkholderia sp. LB400 1.3.1.56 Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and sequence of the encoding gene (bphB) Comamonas testosteroni 1.3.1.56 cis-2,3-Dihydro-2,3-dihydroxybiphenyl dehydrogenase and cis-1,2-dihydro-1,2-dihydroxynaphathalene dehydrogenase catalyze dehydrogenation of the same range of substrates Burkholderia cepacia 1.3.1.56 cis-2,3-Dihydro-2,3-dihydroxybiphenyl dehydrogenase and cis-1,2-dihydro-1,2-dihydroxynaphathalene dehydrogenase catalyze dehydrogenation of the same range of substrates Comamonas testosteroni 1.3.1.56 cis-2,3-Dihydro-2,3-dihydroxybiphenyl dehydrogenase and cis-1,2-dihydro-1,2-dihydroxynaphathalene dehydrogenase catalyze dehydrogenation of the same range of substrates Burkholderia cepacia LB400 1.3.1.56 Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0 A resolution Pseudomonas sp. 1.3.1.56 Degradation of chlorobiphenyls catalyzed by the bph-encoded biphenyl-2,3-dioxygenase and biphenyl-2,3-dihydrodiol-2,3-dehydrogenase of Pseudomonas sp. LB400 Pseudomonas sp. 1.3.1.56 Degradation of chlorobiphenyls catalyzed by the bph-encoded biphenyl-2,3-dioxygenase and biphenyl-2,3-dihydrodiol-2,3-dehydrogenase of Pseudomonas sp. LB400 Pseudomonas sp. LB400 1.3.1.56 Expression, purification, crystallization and preliminary crystallographic studies of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from Pandoraea pnomenusa B-356 Comamonas testosteroni 1.3.1.56 Expression, purification, crystallization and preliminary crystallographic studies of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from Pandoraea pnomenusa B-356 Comamonas testosteroni B-356 1.3.1.56 Genetically modified organisms to remediate polychlorinated biphenyls. Where do we stand? Burkholderia sp. 1.3.1.56 Genetically modified organisms to remediate polychlorinated biphenyls. Where do we stand? Comamonas testosteroni 1.3.1.56 Genetically modified organisms to remediate polychlorinated biphenyls. Where do we stand? Burkholderia sp. LB400