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Information on EC 1.1.7.1 - 4-hydroxybenzoyl-CoA reductase
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1.1.7.1 4-hydroxybenzoyl-CoA reductaseIUBMB Comments
A molybdenum-flavin-iron-sulfur protein that is involved in the anaerobic pathway of phenol metabolism in bacteria. A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor .
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Word Map
- 1.1.7.1
-
denitrifying
- molybdenum
- fad
- xanthine
- thauera
- mo
- benzoate
-
oxygen-sensitive
- aromatica
- ferredoxins
- 3-hydroxybenzoate
-
rhodopseudomonas
-
atp-driven
- dithionite
- 4-hydroxyphenylacetate
- molybdopterins
-
anoxic
-
acid-labile
- viologens
- palustris
- 3-hydroxybenzoyl-coa
-
one-electron
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
4-hbcr, 4-hydroxybenzoyl-coa reductase, 2-hydroxybenzoyl-coa reductase (dehydroxylating), 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxybenzoyl-CoA reductase (dehydroxylating)
-
-
-
-
4-HBCR
4-hydroxybenzoyl-CoA reductase
4-hydroxylbenzoyl-CoA reductase
EC 1.3.7.9
-
-
formerly
-
EC 1.3.99.20
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-
formerly
-
HBCR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin
mechanism
-
benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin
involved in the anaerobic pathway of phenol metabolism in bacteria
-
-
-
benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin
Birch-like mechanism
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benzoyl-CoA + oxidized ferredoxin + H2O = 4-hydroxybenzoyl-CoA + reduced ferredoxin
catalytic cycle with separated two-electron and one-electron transfer steps
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
-
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reduction
oxidation
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-
-
-
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
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SYSTEMATIC NAME
IUBMB Comments
benzoyl-CoA:oxidized ferredoxin oxidoreductase
A molybdenum-flavin-iron-sulfur protein that is involved in the anaerobic pathway of phenol metabolism in bacteria. A ferredoxin with two [4Fe-4S] clusters functions as the natural electron donor [3].
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CAS REGISTRY NUMBER
COMMENTARY
133758-58-4
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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
4-hydroxybenzoyl-CoA + reduced electron donor
benzoyl-CoA + oxidized electron donor + H2O
-
-
-
-
?
protocatechuyl-CoA + oxidized ferredoxin + H2O
3-hydroxybenzoyl-CoA + reduced ferredoxin
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-
-
-
-
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
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-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
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-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
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-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
-
-
-
ir
4-hydroxybenzoyl-CoA + acceptor
benzoyl-CoA + reduced acceptor
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a Birch-like reduction by means of radical intermediates
-
-
?
benzoyl-CoA + oxidized electron donor + H2O
4-hydroxybenzoyl-CoA + reduced electron donor
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-
-
-
?
benzoyl-CoA + oxidized electron donor + H2O
4-hydroxybenzoyl-CoA + reduced electron donor
-
-
-
-
?
benzoyl-CoA + oxidized ferredoxin + H2O
4-hydroxybenzoyl-CoA + reduced ferredoxin
-
-
-
-
?
benzoyl-CoA + oxidized ferredoxin + H2O
4-hydroxybenzoyl-CoA + reduced ferredoxin
-
-
-
-
?
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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
4-hydroxybenzoyl-CoA + reduced electron donor
benzoyl-CoA + oxidized electron donor + H2O
-
-
-
-
?
protocatechuyl-CoA + oxidized ferredoxin + H2O
3-hydroxybenzoyl-CoA + reduced ferredoxin
-
-
-
-
-
benzoyl-CoA + oxidized electron donor + H2O
4-hydroxybenzoyl-CoA + reduced electron donor
-
-
-
-
?
benzoyl-CoA + oxidized electron donor + H2O
4-hydroxybenzoyl-CoA + reduced electron donor
-
-
-
-
?
benzoyl-CoA + oxidized ferredoxin + H2O
4-hydroxybenzoyl-CoA + reduced ferredoxin
-
-
-
-
?
benzoyl-CoA + oxidized ferredoxin + H2O
4-hydroxybenzoyl-CoA + reduced ferredoxin
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
-
two 2Fe-2S clusters, a 4Fe-4S cluster interacting with molybdenum(V)
molybdopterin cytosine dinucleotide
-
harboured by the large alpha-subunit
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
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contains two (2Fe-2S) clusters harboured by the small gamma-subunit and one (4Fe-4S) cluster, harboured by the medium beta-subunit
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
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cyanide inhibition occurs in both the oxidized and reduced state of 4-HBCR, in the reduced state 4-HBCR is reactivated by simple oxidation, in the oxidized state reactivation is only achieved in the presence of sulfide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
60 mg of enriched 4-HBCR is maximally obtained from 200 g of cells with specific activities of 3-5 micromol of 4-OH-BCoA reduced min-1 mg-1
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme is involved in aniline degradation
Show AA Sequence and Transmembrane Helices (1636 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
260000
35000
82000
-
alpha,beta,gamma, 2 * 82000 + 2 * 35000 + 2 * 17000, in vitro translation experiments
85000
-
1 * 85000, alpha-subunit, 1 * 35000, beta-subunit, 1 * 17000, gamma-subunit
17000
-
alpha,beta,gamma, 2 * 82000 + 2 * 35000 + 2 * 17000, in vitro translation experiments
17000
-
1 * 85000, alpha-subunit, 1 * 35000, beta-subunit, 1 * 17000, gamma-subunit
35000
-
alpha,beta,gamma, 2 * 82000 + 2 * 35000 + 2 * 17000, in vitro translation experiments
35000
-
1 * 85000, alpha-subunit, 1 * 35000, beta-subunit, 1 * 17000, gamma-subunit
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
oligomer
trimer
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1 * 85000, alpha-subunit, 1 * 35000, beta-subunit, 1 * 17000, gamma-subunit
hexamer
-
alpha,beta,gamma, 2 * 82000 + 2 * 35000 + 2 * 17000, in vitro translation experiments
hexamer
-
2 * alpha, molybdopterin protein, + 2 * beta, containing one FAD molecule and one 4Fe-4S cluster each, + 2 * gamma subunit, containing two 2Fe-2s clusters, crystallization data
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the structures of dithionite- and azide-bound 4-HBCR are solved at 2.1 and 2.2 A, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
oxygen sensitive, half the activity is lostiin air within a few min
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from extracts of Thauera aromatica, three chromatographic steps, using anion exchange chromatography on DEAE-Sepharose, Hi Load Q-Sepharose and chromatography on Cibacron Blue agarose
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
contains three open reading frames coding for proteins with very high similiarities to 4-HBCR from Thauera aromatica with 85%, 70% and 91% identities respectively
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Glockler, R.; Tschech, A.; Fuchs, G.
Reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA in a denitrifying, phenol-degrading Pseudomonas species
FEBS Lett.
251
237-240
1989
Pseudomonas sp., Pseudomonas sp. K172
brenda
Heider, J.; Boll, M.; Breese, K.; Breinig, S.; Ebenau-Jehle, C.; Feil, U.; Gad'on, N.; Laempe, D.; Leuthner, B.; Mohamed, M.E.S.; Schneider, S.; Burchhardt, G.; Fuchs, G.
Differential induction of enzymes involved in anaerobic metabolism of aromatic compounds in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
170
120-131
1998
Thauera aromatica
brenda
Breese, K.; Fuchs, G.
4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from the denitrifying bacterium Thauera aromatica - prosthetic groups, electron donor, and genes of a member of the molybdenum-flavin-iron-sulfur proteins
Eur. J. Biochem.
251
916-923
1998
Thauera aromatica
brenda
Brackmann, R.; Fuchs, G.
Enzymes of anaerobic metabolism of phenolic compounds. 4-Hydroxybenzoyl-CoA reductase (dehydroxylating) from a denitrifying Pseudomonas species
Eur. J. Biochem.
213
563-571
1993
Pseudomonas sp., Pseudomonas sp. K172
brenda
Gibson, J.; Dispensa, M.; Harwood, C.S.
4-Hydroxybenzoyl coenzyme A reductase (dehydroxylating) is required for anaerobic degradation of 4-hydroxybenzoate by Rhodopseudomonas palustris and shares features with molybdenum-containing hydroxylases
J. Bacteriol.
179
634-642
1997
Rhodopseudomonas palustris
brenda
El Kasmi, A.; Brachmann, R.; Fuchs, G.; Ragsdale, S.W.
Hydroxybenzoyl-CoA reductase: coupling kinetics and electrochemistry to derive enzyme mechanisms
Biochemistry
34
11668-11677
1995
Pseudomonas sp.
brenda
Gallert, C.; Winter, J.
Anaerobic degradation of 4-hydroxybenzoate: reductive dehydroxylation of 4-hydroxybenzoyl-CoA and ATP formation during 4-hydroxybenzoate decarboxylation by the phenol-metabolizing bacteria of a stable, strictly anaerobic consortium
Appl. Microbiol. Biotechnol.
42
408-414
1994
Desulfovibrio sp., Methanospirillum hungatei
-
brenda
Unciuleac, M.; Boll, M.; Warkentin, E.; Ermler, U.
Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin
Acta Crystallogr. Sect. D
60
388-391
2004
Thauera aromatica
brenda
Boll, M.; Fuchs, G.; Meier, C.; Trautwein, A.; El Kasmi, A.; Ragsdale, S.W.; Buchanan, G.; Lowe, D.J.
Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine oxidase family of molybdenum-containing enzymes
J. Biol. Chem.
276
47853-47862
2001
Thauera aromatica
brenda
Unciuleac, M.; Warkentin, E.; Page, C.C.; Boll, M.; Ermler, U.
Structure of a xanthine oxidase-related 4-hydroxybenzoyl-CoA reductase with an additional [4Fe-4S] cluster and an inverted electron flow
Structure
12
2249-2256
2004
Thauera aromatica
brenda
Boll, M.
Key enzymes in the anaerobic aromatic metabolism catalysing Birch-like reductions
Biochim. Biophys. Acta
1707
34-50
2005
Magnetospirillum magnetotacticum, Rhodopseudomonas palustris, Thauera aromatica
brenda
Boll, M.; Schink, B.; Messerschmidt, A.; Kroneck, P.M.H.
Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism
Biol. Chem.
386
999-1006
2005
Azoarcus sp., Azoarcus sp. EbN1, Magnetospirillum magnetotacticum, Rhodopseudomonas palustris, Thauera aromatica
brenda
Johannes, J.; Unciuleac, M.C.; Friedrich, T.; Warkentin, E.; Ermler, U.; Boll, M.
Inhibitors of the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase
Biochemistry
47
4964-4972
2008
Thauera aromatica, Thauera aromatica K172
brenda
Xie, X.; Mller, N.
Enzymes involved in the anaerobic degradation of phenol by the sulfate-reducing bacterium Desulfatiglans anilini
BMC Microbiol.
18
93
2018
Desulfatiglans anilini
brenda
Heider, J.; Fuchs, G.
Anaerobic metabolism of aromatic compounds
Eur. J. Biochem.
243
577-596
1997
Thauera aromatica
brenda
Ding, B.; Schmeling, S.; Fuchs, G.
Anaerobic metabolism of catechol by the denitrifying bacterium Thauera aromatica - a result of promiscuous enzymes and regulators?
J. Bacteriol.
190
1620-1630
2008
Thauera aromatica
brenda
Xie, X.; Spiteller, D.; Huhn, T.; Schink, B.; Mueller, N.
Desulfatiglans anilini initiates degradation of aniline with the production of phenylphosphoamidate and 4-aminobenzoate as intermediates through synthases and carboxylases from different gene clusters
Front. Microbiol.
11
2064
2020
Desulfatiglans anilini
brenda
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