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Information on EC 1.1.1.404 - tetrachlorobenzoquinone reductase for references in articles please use BRENDA:EC1.1.1.404
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IUBMB Comments Contains FMN. The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.
The expected taxonomic range for this enzyme is: Sphingobium chlorophenolicum
Synonyms
2,3,5,6-tetrachlorobenzoquinone reductase, PcpD, TCBQ reductase,
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2,3,5,6-tetrachlorobenzoquinone reductase
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PcpD
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gene name
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TCBQ reductase
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2,3,5,6-tetrachlorohydroquinone + NAD+ = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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2,3,5,6-tetrachlorohydroquinone:NAD+ oxidoreductase
Contains FMN. The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.
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2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
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2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
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2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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the enzyme participates in the degradation of pentachlorophenol
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2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
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2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
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2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
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2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
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cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
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cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
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2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
M9WIZ7
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2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
M9WIZ7
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2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
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the enzyme participates in the degradation of pentachlorophenol
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NADPH
poor activity with NADPH
FMN
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FMN
the putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster
FMN
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the enzyme is a homotrimer containing a flavin and an Fe2S2 cluster in each subunit
[2Fe-2S]-center
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[2Fe-2S]-center
the putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster
[2Fe-2S]-center
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the enzyme is a homotrimer containing a flavin and an Fe2S2 cluster in each subunit
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Iron
protein contains 1.7 mol of iron per mol
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Pentachlorophenol
competitive, 55% loss of activity at 0.1 mM
tetrachlorohydroquinone
activity of PcpD is stimulated by tetrachlorohydroquinone at low concentrations but inhibited at high concentrations. 83% increase in activity at 0.1 mM tetrachlorohydroquinone, 60% loss of activity at 0.2 mM tetrachlorohydroquinone
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tetrachlorohydroquinone
activity of PcpD is stimulated by tetrachlorohydroquinone at low concentrations but inhibited at high concentrations. 83% increase in activity at 0.1 mM tetrachlorohydroquinone, 60% loss of activity at 0.2 mM tetrachlorohydroquinone
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0.0383
2,6-dichloroindophenol
pH 7.6, 22°C
0.0176
cytochrome c
pH 7.6, 22°C
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14.1
2,6-dichloroindophenol
pH 7.6, 22°C
9.1
cytochrome c
pH 7.6, 22°C
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12000
2,3,5,6-tetrachloro-1,4-benzoquinone
pH 7.6, 22°C
368
2,6-dichloroindophenol
pH 7.6, 22°C
510
cytochrome c
pH 7.6, 22°C
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5
70% of maximum activity
8
20% of maximum activity
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UniProt
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UniProt
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UniProt
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UniProt
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UniProt
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metabolism
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the enzyme participates in the degradation of pentachlorophenol
physiological function
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a mutant strain lacking functional PcpD has an impaired ability to remove pentachlorophenol from the medium but removes tetrachlorophenol from the medium at the same rate as does the wild-type strain
physiological function
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TCBQ reductase is the second enzyme in the pentachlorophenol degradation pathway. It rescues the nonproductive diradical complex generated by pentachlorophenol hydroxylase via two fast sequential one-electron transfers
physiological function
tetrachlorohydroquinone reductase PcpD catalyzes the reduction of tetrachlorohydroquinone to tetrachlorohydroquinone. In the presence of PcpD, tetrachlorohydroquinone formed by pentachlorophenol hydroxylase PcpB is sequestered until it is reduced to the less toxic tetrachlorohydroquinone, protecting the bacterium from the toxic effects of tetrachlorohydroquinone and maintaining flux through the pathway. Deletion of pcpD results in increased sensitivity to phenols that are degraded via a benzoquinone intermediate
physiological function
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a mutant strain lacking functional PcpD has an impaired ability to remove pentachlorophenol from the medium but removes tetrachlorophenol from the medium at the same rate as does the wild-type strain
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PCPD_SPHCR
324
0
35598
Swiss-Prot
M9WLE1_SPHCR
323
0
35400
TrEMBL
M9WIZ7_SPHCR
323
0
35474
TrEMBL
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additional information
protein exists as trimer, dynamic light scattering
36000
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homotrimer
3 * 36000, SDS-PAGE, 3 * 36500, mass spectrometry, 3 * 36500, calculated
homotrimer
3 * 36000, calculated
homotrimer
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3 * 36000, SDS-PAGE, 3 * 36500, mass spectrometry, 3 * 36500, calculated
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homotrimer
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3 * 36000, calculated
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homology modeling of structure. The active site is slightly positively charged and situated in a deep pit on the surface. The putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster. It is formed mainly by residues Ser78, Arg79, Phe225, Gly226, Ala227, Ala228, Leu229, Gln275 and the cofactor FMN
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recombinant protein, golden-brown enzyme with a spectrum consistent with the presence of both a flavin and an iron-sulfur cluster
recombinant protein,. Purified enzyme is colorless
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expression in Eshcerichia coli
expression in Pseudomonas aeruginosa
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expression of PcpD is induced in the presence of pentachlorophenol
expression of PcpD is induced in the presence of pentachlorophenol
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expression of PcpD is induced in the presence of pentachlorophenol
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Dai, M.; Rogers, J.B.; Warner, J.R.; Copley, S.D.
A previously unrecognized step in pentachlorophenol degradation in Sphingobium chlorophenolicum is catalyzed by tetrachlorobenzoquinone reductase (PcpD)
J. Bacteriol.
185
302-310
2003
Sphingobium chlorophenolicum (M9WLE1), Sphingobium chlorophenolicum, Sphingobium chlorophenolicum ATCC 39723 (M9WLE1)
brenda
Rudolph, J.; Erbse, A.H.; Behlen, L.S.; Copley, S.D.
A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum
Biochemistry
53
6539-6549
2014
Sphingobium chlorophenolicum (M9WLE1), Sphingobium chlorophenolicum
brenda
Chen, L.; Yang, J.
Biochemical characterization of the tetrachlorobenzoquinone reductase involved in the biodegradation of pentachlorophenol
Int. J. Mol. Sci.
9
198-212
2008
Sphingobium chlorophenolicum (Q47914), Sphingobium chlorophenolicum, Sphingobium chlorophenolicum ATCC 39723 (Q47914)
brenda
Yadid, I.; Rudolph, J.; Hlouchova, K.; Copley, S.D.
Sequestration of a highly reactive intermediate in an evolving pathway for degradation of pentachlorophenol
Proc. Natl. Acad. Sci. USA
110
E2182-E2190
2013
Sphingobium chlorophenolicum (M9WIZ7), Sphingobium chlorophenolicum (M9WLE1), Sphingobium chlorophenolicum, Sphingobium chlorophenolicum RA2 (M9WIZ7)
brenda
Rudolph, J.; Erbse, A.H.; Behlen, L.S.; Copley, S.D.
A radical intermediate in the conversion of pentachlorophenol to tetrachlorohydroquinone by Sphingobium chlorophenolicum
Biochemistry
53
6539-6549
2014
Sphingobium chlorophenolicum
brenda
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