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Enzyme Nomenclature
Information on EC 1.1.1.404 - tetrachlorobenzoquinone reductase
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1.1.1.404 tetrachlorobenzoquinone reductaseIUBMB Comments
Contains FMN. The enzyme, characterized from the bacterium Sphingobium chlorophenolicum, participates in the degradation of pentachlorophenol.
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PcpD
TCBQ reductase
PcpD
-
-
-
-
TCBQ reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3,5,6-tetrachlorohydroquinone + NAD+ = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
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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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
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
-
-
-
?
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 + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
the enzyme participates in the degradation of pentachlorophenol
-
-
?
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+
-
-
-
?
2,3,5,6-tetrachlorohydroquinone + NADP+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADPH + H+
-
-
-
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
-
-
-
?
2,6-dichloroindophenol + NADH + H+
reduced 2,6-dichloroindophenol + NAD+
-
-
-
?
cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
-
-
?
cytochrome c + NADPH + H+
reduced cytochrome c + NADP+
-
-
-
?
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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
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
2,3,5,6-tetrachlorohydroquinone + NAD+
-
-
-
?
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 + NAD+
2,3,5,6-tetrachloro-1,4-benzoquinone + NADH + H+
-
the enzyme participates in the degradation of pentachlorophenol
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
the putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster
FMN
-
the enzyme is a homotrimer containing a flavin and an Fe2S2 cluster in each subunit
[2Fe-2S]-center
the putative binding pocket is adjacent to the cofactor flavin mononucleotide and the 2Fe-2S cluster
[2Fe-2S]-center
-
the enzyme is a homotrimer containing a flavin and an Fe2S2 cluster in each subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12000
2,3,5,6-tetrachloro-1,4-benzoquinone
pH 7.6, 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme participates in the degradation of pentachlorophenol
physiological function
physiological function
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
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A346BCD1_9BURK
328
0
36095
TrEMBL
-
A0A6J5FWJ2_9BURK
324
0
34477
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
additional information
additional information
protein exists as trimer, dynamic light scattering
additional information
-
protein exists as trimer, dynamic light scattering
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
homotrimer
3 * 36000, SDS-PAGE, 3 * 36500, mass spectrometry, 3 * 36500, calculated
homotrimer
-
3 * 36000, SDS-PAGE, 3 * 36500, mass spectrometry, 3 * 36500, calculated
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, golden-brown enzyme with a spectrum consistent with the presence of both a flavin and an iron-sulfur cluster
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of PcpD is induced in the presence of pentachlorophenol
expression of PcpD is induced in the presence of pentachlorophenol
expression of PcpD is induced in the presence of pentachlorophenol
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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