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1,2,4-benzenetriol + O2
maleylacetic acid
2,3-difluorohydroquinone + O2
?
2,5-difluorohydroquinone + O2
?
2,5-dimethylhydroquinone + O2
2-methylmaleylacetone
2,6-dibromohydroquinone + O2
2-bromomaleylacetate + Br-
-
-
-
?
2,6-dichloro-p-hydroquinone + O2
2-chloromaleylacetate + Cl-
-
-
-
?
2,6-dichlorohydroquinone + O2
2-chloromaleylacetate + Cl-
complete conversion of substrate
-
-
?
2,6-dichlorohydroquinone + O2
?
-
-
0.5-0.6 equiv. of chloride is released during turnover of substrate
-
?
2,6-dimethylhydroquinone + O2
2-methylmaleylacetone + ?
-
-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2
?
2-chloro-6-methylhydroquinone
?
-
complete conversion of substrate, yields a mixture of 1,2- and 1,6-cleavage products. The two modes of cleavage have different Km values for oxygen, consistent with a mechanism in which the substrate binds in two catalytically productive orientations
-
?
2-chlorohydroquinone + O2
?
2-ethylhydroquinone + O2
?
2-hexylhydroquinone + O2
?
2-methoxyhydroquinone + O2
?
59% of the activity with hydroquinone
-
-
?
2-methylhydroquinone + O2
?
2-methylhydroquinone + O2
maleylacetone
-
-
-
-
?
2-pentylhydroquinone + O2
?
19% of the activity with hydroquinone
-
-
?
2-propylhydroquinone + O2
?
23% of the activity with hydroquinone
-
-
?
2-tert-butylhydroquinone + O2
?
5% of the activity with hydroquinone
-
-
?
3,5-difluorohydroquinone + O2
?
4-nitrophenol + O2
?
C1I210; C1I209
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
bromohydroquinone + O2
maleylacetate + Br-
-
-
-
?
chlorohydroquinone + O2
?
-
70% of the activity with hydroquinone
-
-
?
chlorohydroquinone + O2
maleylacetate + Cl-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
hydroquinone + O2
4-hydroxymuconic semialdehyde
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
methoxyhydroquinone + O2
?
-
50% of the activity with hydroquinone
-
-
?
methylhydroquinone + O2
?
methylhydroquinone + O2
maleylacetone + ?
-
-
-
?
additional information
?
-
1,2,4-benzenetriol + O2
maleylacetic acid
-
-
-
-
?
1,2,4-benzenetriol + O2
maleylacetic acid
-
-
-
-
?
2,3-difluorohydroquinone + O2
?
-
80% of the activity with hydroquinone
-
-
?
2,3-difluorohydroquinone + O2
?
-
80% of the activity with hydroquinone
-
-
?
2,5-difluorohydroquinone + O2
?
-
75% of the activity with hydroquinone
-
-
?
2,5-difluorohydroquinone + O2
?
-
75% of the activity with hydroquinone
-
-
?
2,5-dimethylhydroquinone + O2
2-methylmaleylacetone
-
-
-
-
?
2,5-dimethylhydroquinone + O2
2-methylmaleylacetone
-
-
-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2
?
less than 2% of the activity with hydroquinone
-
-
?
2-(1-methyl1-octyl)-hydroquinone + O2
?
less than 2% of the activity with hydroquinone
-
-
?
2-chlorohydroquinone + O2
?
-
ring cleavage product is an acylchloride, which reacts with water to give maleylacetate
-
?
2-chlorohydroquinone + O2
?
29% of the activity with hydroquinone
-
-
?
2-chlorohydroquinone + O2
?
29% of the activity with hydroquinone
-
-
?
2-ethylhydroquinone + O2
?
83% of the activity with hydroquinone
-
-
?
2-ethylhydroquinone + O2
?
83% of the activity with hydroquinone
-
-
?
2-hexylhydroquinone + O2
?
less than 2% of the activity with hydroquinone
-
-
?
2-hexylhydroquinone + O2
?
less than 2% of the activity with hydroquinone
-
-
?
2-methylhydroquinone + O2
?
-
-
-
-
?
2-methylhydroquinone + O2
?
-
-
-
-
?
2-methylhydroquinone + O2
?
139% of the activity with hydroquinone
-
-
?
3,5-difluorohydroquinone + O2
?
-
90% of the activity with hydroquinone
-
-
?
3,5-difluorohydroquinone + O2
?
-
90% of the activity with hydroquinone
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
C1I210; C1I209
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
?
benzene-1,4-diol + O2
(2Z,4E)-4-hydroxy-6-oxohexa-2,4-dienoate
-
-
-
?
bromohydroquinone + O2
?
-
30% of the activity with hydroquinone
-
-
?
bromohydroquinone + O2
?
-
30% of the activity with hydroquinone
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
-
-
-
?
hydroquinone + O2
4-hydroxymuconic acid semialdehyde
consumption of an equimolar amount of molecular oxygen
-
-
?
hydroquinone + O2
4-hydroxymuconic semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic semialdehyde
-
-
-
-
?
hydroquinone + O2
4-hydroxymuconic semialdehyde
-
-
-
-
?
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
-
-
-
?
hydroquinone + O2
gamma-hydroxymuconic acid semialdehyde
-
-
-
?
methylhydroquinone + O2
?
-
120% of the activity with hydroquinone
-
-
?
methylhydroquinone + O2
?
substrate binding structure, overview
-
-
?
methylhydroquinone + O2
?
substrate binding structure, overview
-
-
?
additional information
?
-
-
no substrate: hydroxyquinol, catechol, 2-aminophenol,4-aminophenol, protocatechuate, and gentisate
-
-
?
additional information
?
-
-
no substrate: hydroxyquinol, catechol, 2-aminophenol,4-aminophenol, protocatechuate, and gentisate
-
-
?
additional information
?
-
-
YaiA is a hydroquinone dioxygenase that converts hydroquinone putatively to 4-hydroxymuconic semialdehyde in an oxygen-consuming reaction. Hydroquinone and methylhydroquinone are both substrates of YaiA
-
-
?
additional information
?
-
-
2-methylhydroquinone is a slightly better substrate than unsubstituted hydroquinone
-
-
?
additional information
?
-
-
YaiA is a hydroquinone dioxygenase that converts hydroquinone putatively to 4-hydroxymuconic semialdehyde in an oxygen-consuming reaction. Hydroquinone and methylhydroquinone are both substrates of YaiA
-
-
?
additional information
?
-
-
2-methylhydroquinone is a slightly better substrate than unsubstituted hydroquinone
-
-
?
additional information
?
-
-
no substrate: tetrafluorohydroquinone, 1,2,4-trihydroxybenzene, gentisate, catechol, resorcinol, pyrogallol, and phenol
-
-
?
additional information
?
-
-
no substrate: tetrafluorohydroquinone, 1,2,4-trihydroxybenzene, gentisate, catechol, resorcinol, pyrogallol, and phenol
-
-
?
additional information
?
-
exhibits a high degree of substrate specificity for 2,6-disubstituted hydroquinones, with halogens greatly preferred at those positions. The asymmetric substrate 2-chloro-6-methylhydroquinone yields a mixture of 87% 1,2-cleavage and 13% 1,6-cleavage products with different Km values for oxygen, consistent with a mechanism in which the substrate binds in two catalytically productive orientations. Monosubstituted hydroquinones show a limited amount of ring cleavage but rapidly inactivate the enzyme in an O2-dependent fashion, suggesting that oxidation of the Fe(II) may be the cause
-
-
?
additional information
?
-
no substrates: 2,5-dichloro-p-hydroquinone, 6-chlorohydroxyquinol, hydroxyquinol, 2-chloro-p-hydroquinone, catechol, and 4-fluorocatechol
-
-
?
additional information
?
-
enzyme cleaves aromatic rings with two hydroxyl groups ar para positions preferably. No substrate: catechol
-
-
?
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
?
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
?
additional information
?
-
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
?
additional information
?
-
hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes
-
-
?
additional information
?
-
-
hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes
-
-
?
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
?
additional information
?
-
enzyme catalyzes the ring fission of hydroquinone to 4-hydroxymuconic semialdehyde and the degradation of chlorinated and several alkylated hydroquinones
-
-
?
additional information
?
-
hydroquinone 1,2-dioxygenase, a Fe(II) ring cleaving dioxygenase from Sphingomonas sp. strain TTNP3, oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes
-
-
?
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2,2'-dipyridyl
-
inactivation
2,6-dibromophenol
competitive
3,4-dihydroxybenzoate
0.2 mM, 94% inhibition; 0.2 mM, 94% inhibition
3-bromocatechol
inactivation
4-coumaric acid
0.2 mM, 97% inhibition; 0.2 mM, 97% inhibition
4-Hydroxybenzonitrile
-
0.2 mM, no residual activity
4-hydroxycinnamate
-
0.2 mM, no residual activity
bromohydroquinone
-
substrate inhibition
caffeic acid
0.2 mM, 98% inhibition; 0.2 mM, 98% inhibition
catechol
0.2 mM, 93% inhibition; 0.2 mM, 93% inhibition
chlorohydroquinone
-
substrate inhibition
hydrogen peroxide
-
inactivation
Hydroxyhydroquinone
-
0.2 mM, 9% residual activity
methoxyhydroquinone
-
strong substrtae inhibition
o-phenanthroline
-
inactivation
ortho-disubstituted phenols
-
-
phenol
0.2 mM, 98% inhibition; 0.2 mM, 98% inhibition
resorcinol
0.2 mM, 99% inhibition; 0.2 mM, 99% inhibition
vanillate
0.2 mM, 86% inhibition; 0.2 mM, 86% inhibition
Vanillyl alcohol
0.2 mM, 62% inhibition; 0.2 mM, 62% inhibition
4-hydroxybenzoate
-
competitive with hydroquinone
4-hydroxybenzoate
0.2 mM, 46% inhibition; 0.2 mM, 46% inhibition
4-hydroxybenzoate
binding structure, overview
4-nitrophenol
-
0.2 mM, no residual activity
4-nitrophenol
binding structure, overview
additional information
-
4-hydrobenzoate, the competitive inhibitor of the heterotetrameric HapCD hydroquinone dioxygenase of Pseudomonas fluorescens ACB, stabilizes the enzyme
-
additional information
-
weak or no inhibition: 2-hydroxy-, 3-hydroxy-, 2,3-dihydroxy-, 2,5-dihydroxy-, 2,6-dihydroxy-, 3,4-dihydroxy-, 3,4,5-trihydroxy-, 3-chloro-4-hydroxy-, tetrafluoro-4-hydroxy-, 3-amino-4-hydroxy-, 4-hydroxy-3-methoxy-, 4-amino- and methyl 4-hydroxybenzoate; 6-hydroxynicotinate, 4-hydroxypropiophenone, 4-hydroxymandelate, 4-hydroxyphenylglycine, 4-hydroxybenzenesulfonic acid, and 4-methyl-, 4-methoxy-, and 4-aminophenol
-
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?
-
x * 34000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
-
?
-
x * 43300, SDS-PAGE
-
?
x * 19000, subunit PnpC1
?
x * 38000, subunit PnpC2
?
-
x * 19000, subunit PnpC1
-
?
-
x * 38000, subunit PnpC2
-
?
-
x * 36522, electrospray LC-MS
heterotetramer
C1I210; C1I209
2 * 38300, subunit alpha, + 2 * 18000, subunit beta
heterotetramer
2 * 19000, subunit alpha, + 2 * 38000, subunit beta
heterotetramer
-
2 * 19000, subunit alpha, + 2 * 38000, subunit beta
-
tetramer
-
2 * 17800, alpha-subunit, + 2 * 38300, beta-subunit
tetramer
-
2 * 17800, alpha-subunit, + 2 * 38300, beta-subunit
-
tetramer
2 * 38000, large subunit, + 2 * 19000, small subunit
tetramer
-
2 * 38000, large subunit, + 2 * 19000, small subunit
-
additional information
C1I210; C1I209
the PnpCD structure contains a pseudo cupin and an iron metallocenter in the catalytic PnpD. Both the PnpC and the C-terminal domains of PnpD comprise a conserved cupin fold, whereas PnpC cannot form a competent metal binding pocket as can PnpD cupin, structure analysis, overview
additional information
both subunits alpha and beta fold as a cupin, but that of the small alpha subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit of the enzyme crystals
additional information
-
both subunits alpha and beta fold as a cupin, but that of the small alpha subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit of the enzyme crystals
additional information
-
both subunits alpha and beta fold as a cupin, but that of the small alpha subunit lacks a competent metal binding pocket. Two tetramers are present in the asymmetric unit of the enzyme crystals
-
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purified full-length or proteolytically truncated PnpCD in apo form and in complex with Fe3+ or substrate analogue hydroxybenzonitrile and Cd2+, i.e. apo-PnpCD, PnpCD-Fe3+, and PnpCD-Cd2+-HBN, sitting-drop vapor diffusion method, 15-20 mg/ml protein in 10mM Tris-HCl, pH 8.0, and 100 mM NaCl, is mixed with reservoir solution containing 0.2 M sodium thiocyanate, 20% w/v PEG 3350, 20°C, method optimization, X-ray diffraction structure determination and analysis
C1I210; C1I209
generation of a homology model, based on zinc protein PDB entry 1ZSW, which predicts that the tertiary structure of the enzyme differs significantly from that of the extradiol dioxygenases, and that the residues ligating the Fe(II) are H11, H227, and E276
purified enzyme free or in complex with substrate methylhydroquinone under anaerobic conditions, or with inhibitors 4-hydroxybenzoate and 4-nitrophenol, sitting drop vapor diffusion method, mixing of 0.001 ml of 8 mg/ml protein in 25 mM Tris, pH 7.0, 5 mM NaCl, and 0.5 mM ligand, with 0.001 ml of reservoir solution containing 14% PEG 3350, 0.35 M MgCl2, and 0.1 M MES, pH 6.5, 4°C, 1 day, the structure of the free enzyme is obtained by soaking the crystals in a stabilizing solution containing 16% PEG 3350, 0.35 M MgCl2, and 0.1 M MES, pH 6.5, for two days, changing the solution three times, in order to remove the ligands, X-ray diffraction structure determination and analysis at 1.90-2.40 resolution, molecular replacement using the coordinates of PnpCD structure from Pseudomonas sp. strain WBC-3, PDB ID 4ZXA as template, modeling
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E248Q
C1I210; C1I209
site-directed mutagenesis, the mutation results in complete loss of enzyme activity
F264A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
F79A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
L252A
C1I210; C1I209
site-directed mutagenesis, the mutation results in a 70% loss of enzyme activity
L313A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
V315A
C1I210; C1I209
site-directed mutagenesis, the mutation results in a 50% loss of enzyme activity
W230A
C1I210; C1I209
site-directed mutagenesis, the mutation results in a 70% loss of enzyme activity
W273a
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
W76A
C1I210; C1I209
site-directed mutagenesis, the mutation results in almost complete loss of enzyme activity
E276A
less than 6% of wild-type activity
H11A
less than 6% of wild-type activity
H159A
67% of wild-type activity
H227A
less than 6% of wild-type activity
Y266F
about 6% of wild-type activity
E278A
mutation in putative Fe(II)-binding site, complete loss of activity
H162A
mutation in putative Fe(II)-binding site, complete loss of activity
H229A
mutation in putative Fe(II)-binding site, complete loss of activity
additional information
expression of the hydroquinone dioxygenase PnpC1C2 multi-component protein complex in Escherichia coli results in conversion of hydroquinone to 4-hydroxymuconic semialdehyde
additional information
expression of the hydroquinone dioxygenase PnpC1C2 multi-component protein complex in Escherichia coli results in conversion of hydroquinone to 4-hydroxymuconic semialdehyde
additional information
-
expression of the hydroquinone dioxygenase PnpC1C2 multi-component protein complex in Escherichia coli results in conversion of hydroquinone to 4-hydroxymuconic semialdehyde
-
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Kolvenbach, B.A.; Lenz, M.; Benndorf, D.; Rapp, E.; Fousek, J.; Vlcek, C.; Schaeffer, A.; Gabriel, F.L.; Kohler, H.P.; Corvini, P.F.
Purification and characterization of hydroquinone dioxygenase from Sphingomonas sp. strain TTNP3
AMB Express
1
08
2011
Sphingomonas sp. (F8TW82), Sphingomonas sp. (F8TW83), Sphingomonas sp., Sphingomonas sp. TTNP3 (F8TW82), Sphingomonas sp. TTNP3 (F8TW83)
brenda
Xun, L.; Bohuslavek, J.; Cai, M.
Characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723
Biochem. Biophys. Res. Commun.
266
322-325
1999
Sphingobium chlorophenolicum (Q9ZBB0)
brenda
Xu, L.; Resing, K.; Lawson, S.; Babbitt, P.; Copley, S.
Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723
Biochemistry
38
7659-7669
1999
Sphingobium chlorophenolicum
brenda
Machonkin, T.E.; Doerner, A.E.
Substrate specificity of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone 1,2-dioxygenase
Biochemistry
50
8899-8913
2011
Sphingobium chlorophenolicum (Q9ZBB0)
brenda
Shen, W.; Liu, W.; Zhang, J.; Tao, J.; Deng, H.; Cao, H.; Cui, Z.
Cloning and characterization of a gene cluster involved in the catabolism of p-nitrophenol from Pseudomonas putida DLL-E4
Biores. Technol.
101
7516-7522
2010
Pseudomonas putida (C6FI40), Pseudomonas putida (C6FI41), Pseudomonas putida DLL-E4 (C6FI40), Pseudomonas putida DLL-E4 (C6FI41), Pseudomonas putida DLL-E4
brenda
Zhang, S.; Sun, W.; Xu, L.; Zheng, X.; Chu, X.; Tian, J.; Wu, N.; Fan, Y.
Identification of the para-nitrophenol catabolic pathway, and characterization of three enzymes involved in the hydroquinone pathway, in Pseudomonas sp. 1-7
BMC Microbiol.
12
27
2012
Pseudomonas sp.
brenda
Yin, Y.; Zhou, N.Y.
Characterization of MnpC, a hydroquinone dioxygenase likely involved in the meta-nitrophenol degradation by Cupriavidus necator JMP134
Curr. Microbiol.
61
471-476
2010
Cupriavidus necator, Cupriavidus necator JMP 134-1
brenda
Miyauchi, K.; Adachi, Y.; Nagata, Y.; Takagi, M.
Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of gamma-hexachlorocyclohexane in Sphingomonas paucimobilis
J. Bacteriol.
181
6712-6719
1999
Sphingomonas paucimobilis (Q9WXE6)
brenda
Moonen, M.J.; Synowsky, S.A.; van den Berg, W.A.; Westphal, A.H.; Heck, A.J.; van den Heuvel, R.H.; Fraaije, M.W.; van Berkel, W.J.
Hydroquinone dioxygenase from Pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenases
J. Bacteriol.
190
5199-5209
2008
Pseudomonas fluorescens, Pseudomonas fluorescens ACB
brenda
Machonkin, T.E.; Holland, P.L.; Smith, K.N.; Liberman, J.S.; Dinescu, A.; Cundari, T.R.; Rocks, S.S.
Determination of the active site of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone dioxygenase (PcpA)
J. Biol. Inorg. Chem.
15
291-301
2010
Sphingobium chlorophenolicum (Q9ZBB0)
brenda
Ferraroni, M.; Da Vela, S.; Kolvenbach, B.A.; Corvini, P.F.; Scozzafava, A.
The crystal structures of native hydroquinone 1,2-dioxygenase from Sphingomonas sp. TTNP3 and of substrate and inhibitor complexes
Biochim. Biophys. Acta
1865
520-530
2017
Sphingomonas sp. (F8TW82 AND F8TW83), Sphingomonas sp., Sphingomonas sp. TTNP3 (F8TW82 AND F8TW83)
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Liu, S.; Su, T.; Zhang, C.; Zhang, W.M.; Zhu, D.; Su, J.; Wei, T.; Wang, K.; Huang, Y.; Guo, L.; Xu, S.; Zhou, N.Y.; Gu, L.
Crystal structure of PnpCD, a two-subunit hydroquinone 1,2-dioxygenase, reveals a novel structural class of Fe2+-dependent dioxygenases
J. Biol. Chem.
290
24547-24560
2015
Pseudomonas sp. (C1I210 AND C1I209)
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Mancini, S.; Abicht, H.K.; Gonskikh, Y.; Solioz, M.
A copper-induced quinone degradation pathway provides protection against combined copper/quinone stress in Lactococcus lactis IL1403
Mol. Microbiol.
95
645-659
2015
Lactococcus lactis, Lactococcus lactis IL1403
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Zur, J.; Pinski, A.; Michalska, J.; Hupert-Kocurek, K.; Nowak, A.; Wojcieszynska, D.; Guzik, U.
A whole-cell immobilization system on bacterial cellulose for the paracetamol-degrading Pseudomonas moorei KB4 strain
Int. Biodeter. Biodegrad.
149
104919
2020
Pseudomonas moorei, Pseudomonas moorei KB4
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