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Information on EC 1.14.12.18 - biphenyl 2,3-dioxygenase and Organism(s) Paraburkholderia xenovorans and UniProt Accession P37334
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1.14.12.18 biphenyl 2,3-dioxygenaseIUBMB Comments
Requires Fe2+. The enzyme from Burkholderia fungorum LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron centre. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11 (toluene dioxygenase).
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Word Map
- 1.14.12.18
- biphenyls
-
polychlorinated
- pseudoalcaligenes
- xenovorans
-
chlorobiphenyls
-
dihydrodiols
- comamonas
-
rieske-type
- testosteroni
-
pcb-degrading
-
bpdos
-
pcb-contaminated
- yanoikuyae
-
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic
- 2,3-dihydroxybiphenyls
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biphenyl-degrading
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cis-dihydrodiols
- globerulus
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ring-hydroxylating
- pnomenusa
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2,2\'-dichlorobiphenyl
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pandoraea
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polychlorobiphenyls
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biphenyl-utilizing
- synthesis
- beijerinckia
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chlorobenzoates
-
biphenyl-induced
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2,2\',5,5\'-tetrachlorobiphenyl
The taxonomic range for the selected organisms is: Paraburkholderia xenovorans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
biphenyl dioxygenase, bpha1, bph dox, biphenyl 2,3-dioxygenase, bphabc, bphae, biphenyl-2,3-dioxygenase, bphabcd, bpdolb400, 2,3-biphenyl dioxygenase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BDO
-
-
-
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Biphenyl 2,3-dioxygenase
-
-
-
-
biphenyl dioxygenase
BPDO
BPDOLB400
BPH dox
BPO
-
-
-
-
biphenyl dioxygenase
-
-
-
-
BPDO
-
-
-
-
BPH dox
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
biphenyl,NADH:oxygen oxidoreductase (2,3-hydroxylating)
Requires Fe2+. The enzyme from Burkholderia fungorum LB400 (previously Pseudomonas sp.) is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron centre. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11 (toluene dioxygenase).
CAS REGISTRY NUMBER
COMMENTARY
103289-55-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
2,2',3,3'-tetrachlorobiphenyl + NADH + H+ + O2
5,6-dihydro-5,6-dihydroxy-2,2',3,3'-tetrachlorobiphenyl + 4,5-dihydro-4,5-dihydroxy-2,2',3,3'-tetrachlorobiphenyl + NAD+
-
-
-
-
?
2,2',5,5'-tetrachlorobiphenyl + NADH + H+ + O2
3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl + NAD+
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+ + HCl
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + cis-3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + NAD+ + HCl
-
poor substrate
-
-
?
2,3,2',3'-tetrachlorobiphenyl + NADH + H+ + O2
4,5-dihydro-4,5-dihydroxy-2,3,2',3'-tetrachlorobiphenyl + NAD+
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oxygenated onto meta-para carbons 4 and 5
-
-
?
2,3,2',3'-tetrachlorobiphenyl + NADH + H+ + O2
cis-4,5-dihydro-4,5-dihydroxy-2,3,2',3'-tetrachlorobiphenyl + NAD+
-
-
-
-
?
2,4',5-trichlorobiphenyl + NADH + H+ + O2
3,4-dihydro-3,4-dihydroxy-2,5,4'-trichlorobiphenyl + 2',3'-dihydro-2',3'-dihydroxy-2,5,4'-trichlorobiphenyl + NAD+
-
-
-
-
?
2,4,2',4'-tetrachlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2',4,4'-trichlorobiphenyl + NAD+ + HCl
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oxygenated principally onto vicinal ortho-meta carbons 2 and 3
-
-
?
2,4,4'-trichlorobiphenyl + NADH + H+ + O2
2,3-dihydro-2,3-dihydroxy-2',4,4'-trichlorobiphenyl + NAD+
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-
-
-
?
2,6-dichlorobiphenyl + NADH + H+ + O2
2,6-dichloro-2',3'-dihydro-2',3'-dihydroxybiphenyl + ?
-
-
-
-
?
3,3'-dichlorobiphenyl + NADH + O2
5,6-dihydroxy-1-phenylcyclohexa-1,3-diene + 4,5-dihydroxy-1-phenylcyclohexa-1,2-diene + NAD+ + HCl
-
-
-
-
?
biphenyl + NAD(P)H + O2
cis-biphenyl 2,3-dihydrodiol + NAD(P)+
-
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
cis-(2R,3S)-dihydroxy-1-phenylcyclohexa-4,6-diene + NAD+
-
-
-
-
?
biphenyl + NADH + O2
cis-biphenyl 2,3-dihydrodiol + NAD+
-
-
-
-
?
dibenzo-p-dioxin + NADH + O2
2,2',3-trihydroxybiphenyl ether + NAD+
-
-
-
-
?
dibenzofurane + NADH + O2
2,2',3-trihydroxybiphenyl + dihydro-dihydroxy-dibenzofuran + NAD+
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+ small amounts of 2,2',3-trihydroxybiphenyl. 2,2',3-dihydroxybiphenyl results from angular oxygenation, dihydro-dihydroxy-dibenzofuran results from lateral oxygenation
-
?
additional information
?
-
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no activity on toluene and benzene
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-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+ + HCl
-
-
-
-
?
2,2'-dichlorobiphenyl + NADH + H+ + O2
2,3-dihydroxy-2'-chlorobiphenyl + 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl + NAD+ + HCl
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-
the ratio of 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme, 40/60 for the mutant enzymes T335A/F336M, T335A/F336L/I341V and T335A/F336I,80/20 for mutant enzyme T335G, 85/15 for the mutant enzymes T335A and T335A/F336L
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
(1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
2,3-dihydro-dihydroxybiphenyl + NAD+
-
-
-
?
biphenyl + NADH + H+ + O2
cis-(2R,3S)-dihydroxy-1-phenylcyclohexa-4,6-diene + NAD+
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
biphenyl 2,3-dioxygenase catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls
metabolism
metabolism
-
BPDO is one of the most potent biocatalysts of natural origin for the dioxygenation of chlorobiphenyls
metabolism
biphenyl 2,3-dioxygenase catalyzes the initial step in the degradation of biphenyl and some polychlorinated biphenyls
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant BPDOLB400, sitting drop vapour diffusion method, anaerobic conditions, method optimization, 0.002 ml of 8 mg/ml protein in 25 mM HEPES, pH 7.3, containing 0.25 mM ferrous ammonium sulfate, and 2 mM dithiothreitol, is mixed with 0.002 ml of reservoir solution containing 20-25% w/v PEG 8000 or PEG 5000 MME, 50 mM PIPES, pH 6.5, 100 mM ammonium acetate, 5% v/v glycerol, and 0.2% w/v agarose, successful crystallization only occurs at pH 6.5, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution
crystal structure of the BPDOB356/2,6-dichlorobiphenyl complex is determined at 2.4 A resolution
-
purified recombinant BPDOLB400, sitting drop vapour diffusion method, anaerobic conditions, method optimization, 0.002 ml of 8 mg/ml protein in 25 mM HEPES, pH 7.3, containing 0.25 mM ferrous ammonium sulfate, and 2 mM dithiothreitol, is mixed with 0.002 ml of reservoir solution containing 20-25% w/v PEG 8000 or PEG 5000 MME, 50 mM PIPES, pH 6.5, 100 mM ammonium acetate, 5% v/v glycerol, and 0.2% w/v agarose, successful crystallization only occurs at pH 6.5, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution
sitting drop vapor diffusion method, using 20-25% (w/v) PEG 8000 or PEG 5000 MME, 50 mM PIPES pH 6.5, 100 mM ammonium acetate, 5% (v/v) glycerol and 0.2% (w/v) agarose
sitting drop vapor diffusion method, using 2025% (w/v) PEG 8000 or PEG 5000 MME, 50 mM PIPES (pH 6.5), 100 mM ammonium acetate, 5% (v/v) glycerol, and 0.2% (w/v) agarose
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F336M
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the mutant produces principally 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl from 2,2'-dichlorobiphenyl
F370Y
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
L283S
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
M237T
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
S238T
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
T335A
T335A/F336I
-
the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 40/60 for the mutant enzymes
T335A/F336L
-
the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 85/15 for the mutant enzymes
T335A/F336L/I341V
-
the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 40/60 for the mutant enzymes
T335A/F336M
T335G
-
the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 80/20 for the mutant enzymes
T377N
-
lower reactivity toward 2,2-dichlorobiphenyl but unchanged regiospecificity toward this substrate compared to the wild type enzyme
T335A
-
the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 85/15 for the mutant enzymes
T335A
-
the mutant yields 2,3-dihydroxy-2,2'chlorobiphenyl as the major metabolite from 2,2'-dichlorobiphenyl
T335A/F336M
-
the ratio of the product formed from 2,2'-dichlorobiphenyl, 2,3-dihydroxy-2'-chlorobiphenyl to 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl is: 90/10 for the wild-type enzyme and 40/60 for the mutant enzymes
T335A/F336M
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the mutant metabolizes 2,2'-dichlorobiphenyl better than the wild type enzyme to generate principally 3,4-dihydro-3,4-dihydroxy-2,2'-dichlorobiphenyl instead of 2,3-dihydroxy-2'-chlorobiphenyl as produced by the wild type enzyme, the mutant produces 3',4'-dihydroxy-3',4'-dihydro-2,6-dichlorobiphenyl as a major metabolite from 2,6-dichlorobiphenyl
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged subunits alpha and beta and mutant variants from Escherichia coli strain C41(DE3) by affinity chromatography, the tag is cleaved off by thrombin
recombinant His-tagged subunits alpha and beta and mutant variants from Escherichia coli strain C41 (DE3) by affinity chromatography, the tag is cleaved off by thrombin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged subunits alpha and beta and mutant variants in Escherichia coli strain C41(DE3)
based on analyses with Nicotiana benthamiana plants transiently expressing the biphenyl dioxygenase genes (the two subunit oxygenase (BphAE) containing a Rieske-type ironsulfur cluster and a mononuclear iron center, the Rieske-type ferredoxin (BphF), and the FAD-containing ferredoxin reductase (BphG)) from Burkholderia xenovorans LB400 and transgenic Nicotiana tabacum plants transformed with each of these four genes, it can be shown that each of the three biphenyl dioxygenase components can be produced individually as active protein in tobacco plants
-
expression of His-tagged subunits alpha and beta and mutant variants in Escherichia coli strain C41 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
L'Abbee J.B.; Barriault, D.; Sylvestre, M.
Metabolism of dibenzofuran and dibenzo-p-dioxin by the biphenyl dioxygenase of Burkholderia xenovorans LB400 and Comamonas testosteroni B-356
Appl. Microbiol. Biotechnol.
67
506-514
2005
Comamonas testosteroni, Paraburkholderia xenovorans
Barriault, D.; Sylvestre, M.
Evolution of the biphenyl dioxygenase BphA from Burkholderia xenovorans LB400 by random mutagenesis of multiple sites in region III
J. Biol. Chem.
279
47480-47488
2004
Paraburkholderia xenovorans
Barriault, D.; Lepine, F.; Mohammadi, M.; Milot, S.; Leberre, N.; Sylvestre, M.
Revisiting the regiospecificity of Burkholderia xenovorans LB400 biphenyl dioxygenase toward 2,2'-dichlorobiphenyl and 2,3,2',3'-tetrachlorobiphenyl
J. Biol. Chem.
279
47489-47496
2004
Paraburkholderia xenovorans
Zielinski, M.; Kahl, S.; Standfuss-Gabisch, C.; Camara, B.; Seeger, M.; Hofer, B.
Generation of novel-substrate-accepting biphenyl dioxygenases through segmental random mutagenesis and identification of residues involved in enzyme specificity
Appl. Environ. Microbiol.
72
2191-2199
2006
Paraburkholderia xenovorans
Witzig, R.; Junca, H.; Hecht, H.J.; Pieper, D.H.
Assessment of toluene/biphenyl dioxygenase gene diversity in benzene-polluted soils: links between benzene biodegradation and genes similar to those encoding isopropylbenzene dioxygenases
Appl. Environ. Microbiol.
72
3504-3514
2006
Pseudomonas aeruginosa, Burkholderia sp. (O86136), Paraburkholderia xenovorans (P37333), Comamonas testosteroni (Q46372), Comamonas testosteroni (Q8KZP9), Pseudomonas oleovorans (Q52028), Pseudomonas sp. (Q52438), Rhodococcus globerulus (Q52757), Rhodococcus sp. (Q53122), Rhodococcus erythropolis (Q79EP8), Pseudomonas aeruginosa JI104, Rhodococcus globerulus P6 (Q52757), Pseudomonas oleovorans KF707 (Q52028), Rhodococcus erythropolis TA421 (Q79EP8)
Suenaga, H.; Sato, M.; Goto, M.; Takeshita, M.; Furukawa, K.
Steady-state kinetic characterization of evolved biphenyl dioxygenase, which acquired novel degradation ability for benzene and toluene
Biosci. Biotechnol. Biochem.
70
1021-1025
2006
Pseudomonas oleovorans, Paraburkholderia xenovorans
Vezina, J.; Barriault, D.; Sylvestre, M.
Family shuffling of soil DNA to change the regiospecificity of Burkholderia xenovorans LB400 biphenyl dioxygenase
J. Bacteriol.
189
779-788
2007
Paraburkholderia xenovorans
Mohammadi, M.; Chalavi, V.; Novakova-Sura, M.; Laliberte, J.; Sylvestre, M.
Expression of bacterial biphenyl-chlorobiphenyl dioxygenase genes in tobacco plants
Biotechnol. Bioeng.
97
496-505
2007
Paraburkholderia xenovorans
Gomez-Gil, L.; Kumar, P.; Barriault, D.; Bolin, J.T.; Sylvestre, M.; Eltis, L.D.
Characterization of biphenyl dioxygenase of Pandoraea pnomenusa B-356 as a potent polychlorinated biphenyl-degrading enzyme
J. Bacteriol.
189
5705-5715
2007
Paraburkholderia xenovorans, Pandoraea pnomenusa, Pandoraea pnomenusa B-356
Kumar, P.; Gomez-Gil, L.; Mohammadi, M.; Sylvestre, M.; Eltis, L.D.; Bolin, J.T.
Anaerobic crystallization and initial X-ray diffraction data of biphenyl 2,3-dioxygenase from Burkholderia xenovorans LB400: addition of agarose improved the quality of the crystals
Acta Crystallogr. Sect. F
67
59-62
2011
Paraburkholderia xenovorans, Paraburkholderia xenovorans (P37333), Paraburkholderia xenovorans (P37334)
Kumar, P.; Mohammadi, M.; Viger, J.F.; Barriault, D.; Gomez-Gil, L.; Eltis, L.D.; Bolin, J.T.; Sylvestre, M.
Structural insight into the expanded PCB-degrading abilities of a biphenyl dioxygenase obtained by directed evolution
J. Mol. Biol.
405
531-547
2011
Paraburkholderia xenovorans
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