Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.2.7.4 - anaerobic carbon-monoxide dehydrogenase and Organism(s) Carboxydothermus hydrogenoformans and UniProt Accession Q9F8A8

for references in articles please use BRENDA:EC1.2.7.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Carboxydothermus hydrogenoformans
UNIPROT: Q9F8A8
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Carboxydothermus hydrogenoformans
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
CO dehydrogenase complex II
-
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
-
-
-
-
Ni,Fe-dependent carbon monoxide dehydrogenase
-
-
Ni-Fe carbon monoxide dehydrogenase II
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
anaerobic CO dehydrogenases catalyze the reversible oxidation of CO to CO2 at a complex Ni-, Fe-, and S-containing metal center called cluster C
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
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 + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
-
-
-
?
CO + H2O
CO2 + H2
show the reaction diagram
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
H2 + reduced methyl viologen
methyl viologen
show the reaction diagram
-
-
-
-
r
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
CO2 + H2
show the reaction diagram
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
show the reaction diagram
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ni-4Fe-5S center
-
active site cluster
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S2-
contains a [NiFe4S5] center called cluster C
Nickel
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
slow binding inhibitor of CODH
CO
-
45% CO in headspace, 50% inhibition
cyanide
potassium cyanide
-
competitive inhibitor of reduced CODHII with respect to the substrate CO, inhibition of dithionite- or Ti(III) citrate-reduced CODHII by potassium cyanide is fully reversible since the enzyme can be completely reactivated, sodium sulfide has no effect on the reactivation of cyanide-inhibited CODHII in the presence of dithionite
S2-
-
partial inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ti(III)citrate
-
1mM for 1 min at 65°C, 45fold increase in initial activity
additional information
-
CooC proteins are ATPases involved in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenases
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
methyl viologen
-
at 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1500 - 15900
CO
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0217
cyanide
-
at 23°C, in 4 mM dithionite, and 4 mM dithiothreitol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14000
-
carbon monoxide dehydrogenase II
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
both for enzyme and complex
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
x * 70000, SDS-PAGE
120000
-
gel filtration, enzyme
450000
-
gel filtration, complex
62000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 62000, SDS-PAGE, enzyme
octamer
-
2 * 62000, enzyme, + electron transfer protein CooF and membrane bound [Ni-Fe] hydrogenase, six differentsubunits
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
carbon monoxide dehydrogenase II, hanging drop vapor diffusion, 20% 2-propanol, 20% polyethylene glycol 3000, 100 mM HEPES, pH 7.5
-
in presence of dithiothreitol or dithionite and under an atmosphere of N2 or CO
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C56A
-
devoid of CO oxidation activity
K563L
-
very low CO oxidation activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Cosmogel His-Accept column chromatography, and gel filtration
carbon monoxide dehydrogenase II
-
Ni-NTA agarose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli Rosetta2 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dobbek, H.; Svetlitchnyi, V.; Gremer, L.; Huber, R.; Meyer, O.
Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
Science
293
1281-1285
2001
Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Soboh, B.; Linder, D.; Hedderich, R.
Purification and catalytic properties of a CO-oxidizing:H2-evolving enzyme complex from Carboxydothermus hydrogenoformans
Eur. J. Biochem.
269
5712-5721
2002
Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Dobbek, H.; Svetlitchnyi, V.; Liss, J.; Meyer, O.
Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase
J. Am. Chem. Soc.
126
5382-5387
2004
Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Lindahl, P.A.
Implications of a carboxylate-bound C-cluster structure of carbon monoxide dehydrogenase
Angew. Chem.
47
4054-4056
2008
Carboxydothermus hydrogenoformans, Moorella thermoacetica, Rhodospirillum rubrum
Manually annotated by BRENDA team
Seravalli, J.; Ragsdale, S.W.
13C NMR characterization of an exchange reaction between CO and CO2 catalyzed by carbon monoxide dehydrogenase
Biochemistry
47
6770-6781
2008
Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Ha, S.W.; Korbas, M.; Klepsch, M.; Meyer-Klaucke, W.; Meyer, O.; Svetlitchnyi, V.
Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans
J. Biol. Chem.
282
10639-10646
2007
Carboxydothermus hydrogenoformans, Carboxydothermus hydrogenoformans Z-2901 / DSM 6008
Manually annotated by BRENDA team
Jeoung, J.H.; Dobbek, H.
Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase
Science
318
1461-1464
2007
Carboxydothermus hydrogenoformans (Q9F8A8), Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Jeoung, J.; Dobbek, H.
Structural basis of cyanide inhibition of Ni, Fe-containing carbon monoxide dehydrogenase
J. Am. Chem. Soc.
131
9922-9923
2009
Carboxydothermus hydrogenoformans (Q9F8A8), Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Jeoung, J.H.; Giese, T.; Gruenwald, M.; Dobbek, H.
Crystal structure of the ATP-dependent maturation factor of Ni,Fe-containing carbon monoxide dehydrogenases
J. Mol. Biol.
396
1165-1179
2010
Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team
Inoue, T.; Yoshida, T.; Wada, K.; Daifuku, T.; Fukuyama, K.; Sako, Y.
A simple, large-scale overexpression method of deriving carbon monoxide dehydrogenase II from thermophilic bacterium Carboxydothermus hydrogenoformans
Biosci. Biotechnol. Biochem.
75
1392-1394
2011
Carboxydothermus hydrogenoformans (Q9F8A8), Carboxydothermus hydrogenoformans, Carboxydothermus hydrogenoformans DSM 6008 (Q9F8A8)
Manually annotated by BRENDA team
Majumdar, A.
Bioinorganic modeling chemistry of carbon monoxide dehydrogenases: description of model complexes, current status and possible future scopes
Dalton Trans.
43
12135-12145
2014
Carboxydothermus hydrogenoformans
Manually annotated by BRENDA team