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Information on EC 1.2.7.4 - anaerobic carbon-monoxide dehydrogenase and Organism(s) Afipia carboxidovorans and UniProt Accession P19921

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IUBMB Comments
This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl-CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [4Fe-4S] D-cluster; and two [4Fe-4S] B-clusters. In methanogenic archaea additional [4Fe-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase.
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Afipia carboxidovorans
UNIPROT: P19921 not found.
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The taxonomic range for the selected organisms is: Afipia carboxidovorans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
CO
+
H2O
+
2
oxidized ferredoxin
=
CO2
+
2
reduced ferredoxin
+
2
H+
+
+
2
=
+
2
+
2
Synonyms
carbon monoxide dehydrogenase, co dehydrogenase, co-dh, co dehydrogenase/acetyl-coa synthase, co dehydrogenase complex, ni-codh, codh ii, codh-ii, acetyl-coa synthase/carbon monoxide dehydrogenase, ni-containing carbon monoxide dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carbon dioxide/carbon monoxide oxidoreductase
-
-
-
-
Carbon monoxide dehydrogenase
-
-
-
-
carbon monoxide dehydrogenase-corrinoid enzyme complex
-
-
-
-
Carbon monoxide oxidoreductase
-
-
-
-
Cdh
-
-
-
-
CO dehydrogenase
CO dehydrogenase/acetyl-CoA synthase
-
-
-
-
Co-DG
-
-
-
-
Dehydrogenase, carbon monoxide
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
mechnaism via thiocarbonate-like intermediate state
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
carbon-monoxide,water:ferredoxin oxidoreductase
This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl-CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [4Fe-4S] D-cluster; and two [4Fe-4S] B-clusters. In methanogenic archaea additional [4Fe-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase.
CAS REGISTRY NUMBER
COMMENTARY hide
64972-88-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
CO + H2O + acceptor
CO2 + reduced acceptor + H+
show the reaction diagram
-
-
-
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
show the reaction diagram
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
CO + H2O + methylene blue
CO2 + reduced methylene blue
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
CO + H2O + acceptor
CO2 + reduced acceptor + H+
show the reaction diagram
-
-
-
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
show the reaction diagram
-
a proton gradient across the cytoplasmic membrane is generated by channeling the electrons formed via cytochrome b561 into a CO-insensitive respiratory chain
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin adenine dinucleotide
molybdopterin
-
-
molybdopterin cytosine dinucleotide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
Fe2+
-
the enzyme contains iron
Molybdenum
[2Fe-2S]-center
the small subunit contains two [2Fe-2S] centers
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00295 - 0.0107
methylene blue
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.2 - 93.3
methylene blue
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2780 - 8700
methylene blue
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17800
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
273500
-
deduced from amino acid sequence
30200
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
88700
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion, 800 mM KH2PO4, 800 mM NaH2PO4, 2% 2-methyl-2,4-pentanediol, 100 mM HEPES, pH 7.3
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q-Sepharose column chromatography and Sephacryl S-300 gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schubel, U.; Kraut, M.; Morsdorf, G.; Meyer, O.
Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans
J. Bacteriol.
177
2197-2203
1995
Afipia carboxidovorans
Manually annotated by BRENDA team
Dobbek, H.; Gremer, L.; Meyer, O.; Huber, R.
Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
Afipia carboxidovorans
Manually annotated by BRENDA team
Dobbek, H.; Gremer, L.; Kiefersauer, R.; Huber, R.; Meyer, O.
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution
Proc. Natl. Acad. Sci. USA
99
15971-15976
2002
Afipia carboxidovorans
Manually annotated by BRENDA team
Groysman, S.; Majumdar, A.; Zheng, S.; Holm, R.
Reactions of monodithiolene tungsten(VI) sulfido complexes with copper(I) in relation to the structure of the active site of carbon monoxide dehydrogenase
Inorg. Chem.
49
1082-1089
2010
Afipia carboxidovorans
Manually annotated by BRENDA team
Wilcoxen, J.; Snider, S.; Hille, R.
Substitution of silver for copper in the binuclear Mo/Cu center of carbon monoxide dehydrogenase from Oligotropha carboxidovorans
J. Am. Chem. Soc.
133
12934-12936
2011
Afipia carboxidovorans (P19919 and P19920 and P19921), Afipia carboxidovorans
Manually annotated by BRENDA team
Zhang, B.; Hemann, C.F.; Hille, R.
Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans
J. Biol. Chem.
285
12571-12578
2010
Afipia carboxidovorans (P19919 and P19920 and P19921), Afipia carboxidovorans
Manually annotated by BRENDA team