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Information on EC 1.3.7.8 - benzoyl-CoA reductase
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1.3.7.8 benzoyl-CoA reductaseIUBMB Comments
An iron-sulfur protein. Requires Mg2+ or Mn2+. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.
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Word Map
- 1.3.7.8
- benzoate
- thauera
-
denitrifying
- aromatica
- analysis
-
dearomatization
-
atp-driven
- metallireducens
- azoarcus
-
benzoyl-coenzyme
-
geobacter
-
nonaromatic
-
dienoyl-coa
-
benzoate-induced
- syntrophus
-
ketyl
- magnetospirillum
-
benzoate-coa
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
benzoyl-coa reductase, benzoyl-coa reductase (dearomatizing), bambcdefghi complex, class i bcr, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP-dependent benzoyl-CoA reductase (class I)
ATP-dependent class I benzoyl-CoA reductase
BCR
benzoyl-CoA reductase
class I BCR
halobenzoyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
-
-
-
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
ATP-binding switch is rather fast, reverse switch back of MgADP-bound enzyme is considered rate-limiting, binding of nucleotides does not affect redox potential of 4Fe-4S clusters
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
ATP-hydrolysis-driven electron transfer with transient formation of a phosphorylated enzyme, ATPase- and autophosphatase-partial activities exhibit identical redox dependencies
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
Birch-like mechanism
-
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate = benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
Birch-like reduction with base-catalyzed rearrangement to 1,5-diene
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
cyclohexa-1,5-diene-1-carbonyl-CoA:ferredoxin oxidoreductase (aromatizing, ATP-forming)
An iron-sulfur protein. Requires Mg2+ or Mn2+. Inactive towards aromatic acids that are not CoA esters but will also catalyse the reaction: ammonia + acceptor + 2 ADP + 2 phosphate = hydroxylamine + reduced acceptor + 2 ATP + H2O. In the presence of reduced acceptor, but in the absence of oxidizable substrate, the enzyme catalyses the hydrolysis of ATP to ADP plus phosphate.
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CAS REGISTRY NUMBER
COMMENTARY
176591-18-7
-
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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-amino-benzoyl-CoA + reduced methyl viologen + ATP
2-amino-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 11% of the velocity of benzoyl-CoA
-
?
2-aminobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 18% of the activity relative to benzoyl-CoA
-
?
2-chloro-benzoyl-CoA + reduced methyl viologen + ATP
2-chloro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 106% of the velocity of benzoyl-CoA
-
?
2-fluoro-benzoyl-CoA + reduced methyl viologen + ATP
2-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 145% of the velocity of benzoyl-CoA
-
?
2-hydroxy-benzoyl-CoA + reduced methyl viologen + ATP
2-hydroxy-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 64% of the velocity of benzoyl-CoA
-
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-fluoro-benzoyl-CoA + reduced methyl viologen + ATP
3-fluoro-cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
at 31% of the velocity of benzoyl-CoA
-
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 23% of the activity relative to benzoyl-CoA
-
?
3-hydroxybenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 12% of the activity relative to benzoyl-CoA
-
?
3-methylbenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 12% of the activity relative to benzoyl-CoA
-
?
4-hydroxybenzoyl-CoA + reduced methyl viologen + ATP
4-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA + oxidized methyl viologen + ADP + phosphate
-
at 5% of the activity relative to benzoyl-CoA
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + ferredoxin + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced methyl viologen + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + methyl viologen + ADP + phosphate
-
-
-
?
furan-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 28% of the velocity of benzoyl-CoA
-
?
pyridine-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 67% of the velocity of benzoyl-CoA
-
?
pyridine-4-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 41% of the velocity of benzoyl-CoA
-
?
thiophene-2-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 144% of the velocity of benzoyl-CoA
-
?
thiophene-3-carbonyl-CoA + reduced methyl viologen + ATP
? + methyl viologen + ADP + phosphate
-
at 10% of the velocity of benzoyl-CoA
-
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 78% of the activity relative to benzoyl-CoA
-
?
2-fluorobenzoyl-CoA + reduced methyl viologen + ATP
?
-
at 10% of the activity relative to benzoyl-CoA
-
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
3-fluorobenzoyl-CoA is converted only to the fluorinated cyclic dienoyl-CoA compound
-
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
ir
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
acceptor: Ti3+, reduced methyl viologen
-
?
benzoyl-CoA + reduced acceptor + ATP
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
ir
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
the enzyme is involved in the anaerobic catabolism of benzoate
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
rate-limiting enzyme of anaerobic benzoate degradation. badM encodes a transcriptional repressor of benzoyl-CoA reductase gene expression. BadM controls gene expression from the benzoyl-CoA reductase promoter in concert with two transcriptional activators
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
the enzyme is involved in the anaerobic catabolism of benzoate
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
?
additional information
?
-
-
benzoyl-CoA is dearomatized into cyclohexa-1,5-diene-carboxyl-CoA in an ATP-independent reaction cycle
-
?
additional information
?
-
-
in absence of benzoyl-CoA the enzyme exhibits oxygen-sensitive ATPase activity
-
?
additional information
?
-
-
no substrate: furan-3-carbonyl-CoA, pyrrole-2-carbonyl-CoA, pyridine-4-carbonyl-CoA, 4-fluoro-benzoyl-CoA
-
?
additional information
?
-
-
reduction of aromatic ring requires 2 mol of ATP per mol of benzoyl-CoA
-
?
additional information
?
-
-
the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
-
?
additional information
?
-
-
reactions under anaerobic conditions
-
?
additional information
?
-
-
the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
-
?
additional information
?
-
-
reactions under anaerobic conditions
-
?
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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
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
benzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
benzoyl-CoA + reduced ferredoxin + ATP + H2O
cyclohexa-1,5-diene-1-carboxyl-CoA + oxidized ferredoxin + ADP + phosphate
-
-
-
-
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
3-bromobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-bromocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
3-chlorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-chlorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
3-fluorobenzoyl-CoA + reduced ferredoxin + 2 ATP + 2 H2O
3-fluorocyclohexa-1,5-diene-1-carbonyl-CoA + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
-
?
Benzoyl-CoA + reduced acceptor + ATP
?
-
key enzyme of anaerobic aromatic metabolism
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
the enzyme is involved in the anaerobic catabolism of benzoate
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
rate-limiting enzyme of anaerobic benzoate degradation. badM encodes a transcriptional repressor of benzoyl-CoA reductase gene expression. BadM controls gene expression from the benzoyl-CoA reductase promoter in concert with two transcriptional activators
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
the enzyme is involved in the anaerobic catabolism of benzoate
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
benzoyl-CoA + reduced acceptor + ATP + H2O
cyclohexa-1,5-diene-1-carbonyl-CoA + acceptor + ADP + phosphate
-
central enzyme in the anaerobic degradation of organic carbon
-
-
?
additional information
?
-
-
benzoyl-CoA is dearomatized into cyclohexa-1,5-diene-carboxyl-CoA in an ATP-independent reaction cycle
-
-
?
additional information
?
-
-
the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
-
-
?
additional information
?
-
-
the enzyme catalyzes ATP-dependent reductive dehalogenation of 3-chloro/3-bromobenzoyl-CoA to benzoyl-CoA, whereas 3-fluorobenzoyl-CoA is converted to a fluorinated cyclic dienoyl-CoA compound. Reductive dechlorination/debromination of 3-Cl-/3-Br-benzoyl-CoA catalyzed by class I BCR yielding benzoyl-CoA, the latter is subsequently dearomatized by the same enzyme. The elimination of HCl/HBr may occur enzymatically or spontaneously
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Mg2+
Iron
-
contains two separate [2Fe-2S]clusters and two interacting [4Fe-4S]clusters
Iron
-
contains 10.8 mol Fe and 10.5 mol acid-labile sulfur per mol of enzyme
Mg2+
-
required, reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 5'-[beta,gamma-methylene]triphosphate
-
inhibition only at high concentration, above 10 mM, in presence of 5 mM MgATP2-
Ti(III)-citrate
-
required, reductive dehalogenation of 3-chlorobenzoyl-CoA is oxygen sensitive and strictly dependent on the presence of ATP and Ti(III)-citrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
detailed kinetic analysis
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.022
0.025
0.0275
0.0335
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C
0.041
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30°C
0.045
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C
0.022
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C
0.022
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30°C
0.025
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C
0.025
-
specific activtity with 3-chloro-halogenated benzoyl-CoA as substrate with extracts from cells grown on benzoate, pH 7.3, 30°C
0.0275
-
specific activtity with 3-bromo-halogenated benzoyl-CoA as substrate with extracts from cells grown on 3-bromobenzoate, pH 7.3, 30°C
0.0275
-
specific activtity with benzoyl-CoA as substrate with extracts from cells grown on 3-chlorobenzoate, pH 7.3, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6 - 8.2
-
50% of maximal activity at pH 6.6 and 8.2, less than 10% of maximal activity at pH 6.2 and 8.7
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
putative benzoyl-CoA reductase, gene name: bzdQ
SwissProt
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
subunit of benzoyl-CoA reductase, gene name: bzdN
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name: bzdO
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name: bzdP
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name: bzdQ
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badD
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badE
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badF
SwissProt
brenda
subunit of benzoyl-CoA reductase, gene name badG
SwissProt
brenda
-
-
-
brenda
A-subunit of benzoyl-CoA reductase; all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
SwissProt
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
all the Thauera strains and the isolates from the genera Acidovorax, Bradyrhizobium, Paracoccus, Ensifer, and Pseudomonas have bcr-type benzoyl-CoA reductases with amino acid sequence similarities of more than 97%
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cells grown on mixtures of non-aromatic acids plus benzoate contain higher amounts of the enzyme as compared to cells grown on the nonaromatic acids alone
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
additional information
metabolism
-
proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview
metabolism
-
proposed role of class I benzoyl-CoA reductase in the metabolism of halobenzoates, overview
additional information
-
3-chloro/3-bromobenzoyl-CoA dehalogenation/elimination activity is equally present in extracts from Thauera chlorobenzoica grown on 3-chlorobenzoate and benzoate suggesting that no 3-Cl-benzoate-specific class I BCR is induced
additional information
-
3-chloro/3-bromobenzoyl-CoA dehalogenation/elimination activity is equally present in extracts from Thauera chlorobenzoica grown on 3-chlorobenzoate and benzoate suggesting that no 3-Cl-benzoate-specific class I BCR is induced
Show AA Sequence and Transmembrane Helices (711 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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
-
reductive dehalogenase activity is not specifically induced by the halogenated aromatic growth substrates
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
analysis
-
the detection of benzoyl-CoA reductase genes from bacterial pure cultures and environmental samples can be used to determine the genetic capability for anaerobic degradation of aromatic compounds and to monitor the anaerobic degradation of many different aromatic compounds in the environment. Sequence divergence of benzoyl-CoA reductase genes could be used to identify and distinguish among different bacterial populations degrading aromatic compounds in various environments. Microarray or real-time PCR amplification with specific primers for different types of benzoyl-CoA reductase genes could be applicable in environmental studies to determine which types are dominant and activated in particular environmental conditions and to evaluate the population response to variation in environmental factors. The first step in this approach is described
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
Anaerobic metabolism of L-phenylalanine via benzoyl-CoA in the denitrifying bacterium Thauera aromatica
Arch. Microbiol.
168
310-320
1997
Thauera aromatica
brenda
Boll , M.; Fuchs, G.
Identification, and characterization of the natural electron donor ferredoxin and of FAD as a possible prosthetic group of benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism
Eur. J. Biochem.
251
946-954
1998
Thauera aromatica
brenda
Boll, M.; Albracht, S.S.P.; Fuchs, G.
Benzoyl-CoA reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. A study of adenosinetriphosphatase activity, ATP stoichiometry of the reaction and EPR properties of the enzyme
Eur. J. Biochem.
244
840-851
1997
Thauera aromatica, Thauera aromatica K172
brenda
Boll, M.; Fuchs, G.
Benzoyl-coenzyme A reductase (dearomatizing), a key enzyme of anaerobic aromatic metabolism. ATP dependence of the reaction, purification and some properties of the enzyme from Thaurea aromatica strain K172
Eur. J. Biochem.
234
921-933
1995
Thauera aromatica
brenda
Breese, K.; Boll, M.; Alt-Morbe, J.; Schagger, H.; Fuchs, G.
Genes coding the benzoyl-CoA pathway of anaerobic metabolism in the bacterium Thauera aromatica
Eur. J. Biochem.
256
148-154
1998
Thauera aromatica
brenda
Koch, J.; Fuchs, G.
Enzymatic reduction of benzoyl-CoA to acyclic compounds a key reaction in anaerobic aromatic metabolism
Eur. J. Biochem.
205
195-202
1992
Pseudomonas sp.
brenda
Boll, M.; Laempe, D.; Eisenreich, W.; Bachers, A.; Mittelberger, T.; Heinze, J.; Fuchs, G.
Nonaromatic products from anoxic conversion of benzoyl-CoA with benzoyl-CoA reductase and cyclohexa-1,5-diene-1-carbonyl-CoA hydratase
J. Biol. Chem.
275
21889-21895
2000
Thauera aromatica
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
Mobitz, H.; Friedrich, T.; Boll, M.
Substrate binding and reduction of benzoyl-CoA reductase: evidence for nucleotide-dependent conformational changes
Biochemistry
43
1376-1385
2004
Thauera aromatica
brenda
Unciuleac, M.; Boll, M.
Mechanism of ATP-driven electron transfer catalyzed by the benzene ring-reducing enzyme benzoyl-CoA reductase
Proc. Natl. Acad. Sci. USA
98
13619-13624
2001
Thauera aromatica
brenda
Song, B.; Ward, B.B.
Genetic diversity of benzoyl coenzyme a reductase genes detected in denitrifying isolates and estuarine sediment communities
Appl. Environ. Microbiol.
71
2036-2045
2005
Acidovorax sp., Magnetospirillum magnetotacticum, Thauera selenatis, Thauera chlorobenzoica, Aromatoleum toluvorans, Aromatoleum toluclasticum, Rhodopseudomonas palustris (O07460), Rhodopseudomonas palustris (O07461), Rhodopseudomonas palustris (O07462), Rhodopseudomonas palustris (O07463), Rhodopseudomonas palustris, Thauera aromatica (O87876), Thauera aromatica, Aromatoleum tolulyticum (Q4Z8X5), Aromatoleum evansii (Q8VUG0), Aromatoleum evansii (Q8VUG1), Aromatoleum evansii (Q8VUG2), Aromatoleum evansii (Q8VUG3), Aromatoleum evansii, Thauera selenatis 3CB-1, Acidovorax sp. 2FB7, Thauera chlorobenzoica 3CB-1
brenda
Peres, C.M.; Harwood, C.
BadM is a transcriptional repressor and one of the three regulators that control benzoyl coenzyme A reductase gene expression in Rhodopseudomonas palustris
J. Bacteriol.
188
8662-8665
2006
Rhodopseudomonas palustris
brenda
Carmona, M.; Diaz, E.
Iron-reducing bacteria unravel novel strategies for the anaerobic catabolism of aromatic compounds
Mol. Microbiol.
58
1210-1215
2005
Azoarcus sp., Thauera aromatica
brenda
Thiele, B.; Rieder, O.; Golding, B.T.; Mueller, M.; Boll, M.
Mechanism of enzymatic Birch reduction: stereochemical course and exchange reactions of benzoyl-CoA reductase
J. Am. Chem. Soc.
130
14050-14051
2008
Thauera aromatica
brenda
Heintz, D.; Gallien, S.; Wischgoll, S.; Ullmann, A.K.; Schaeffer, C.; Kretzschmar, A.K.; van Dorsselaer, A.; Boll, M.
Differential membrane proteome analysis reveals novel proteins involved in the degradation of aromatic compounds in Geobacter metallireducens
Mol. Cell. Proteomics
8
2159-2169
2009
Geobacter metallireducens
brenda
Kuntze, K.; Kiefer, P.; Baumann, S.; Seifert, J.; von Bergen, M.; Vorholt, J.; Boll, M.
Enzymes involved in the anaerobic degradation of meta-substituted halobenzoates
Mol. Microbiol.
82
758-769
2011
Thauera chlorobenzoica, Thauera chlorobenzoica 3CB-1
brenda
Schmid, G.; Rene, S.B.; Boll, M.
Enzymes of the benzoyl-coenzyme A degradation pathway in the hyperthermophilic archaeon Ferroglobus placidus
Environ. Microbiol.
17
3289-3300
2015
Ferroglobus placidus
brenda
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