Any feedback?
Information on EC 1.2.7.4 - anaerobic carbon-monoxide dehydrogenase and Organism(s) Moorella thermoacetica and UniProt Accession P27989
for references in articles please use BRENDA:EC1.2.7.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.7.4 anaerobic carbon-monoxide dehydrogenaseIUBMB 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
Word Map
- 1.2.7.4
- co2
-
codhs
- nickel
-
acetogenic
- thermoaceticum
- rubrum
- rhodospirillum
- methanosarcina
- carboxydothermus
- hydrogenoformans
- carboxidovorans
-
c-clusters
-
oligotropha
-
wood-ljungdahl
-
co-dependent
-
methanogenesis
-
carboxydotrophic
-
co-oxidizing
- hydrogenases
- barkeri
-
sulfate-reducing
-
nickel-dependent
- acetobacterium
-
nifes
-
molybdenum-containing
-
hydrogenogenic
-
acetogenesis
-
nickel-containing
-
syngas
-
methyl-coenzyme
- moorella
-
square-planar
-
homoacetogenic
-
overpotential
-
acetate-grown
-
fe-containing
-
electrocatalysts
- analysis
-
hydrogenophaga
- methyltetrahydrofolate
-
cubane-type
The taxonomic range for the selected organisms is: Moorella thermoacetica
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carbon monoxide dehydrogenase/acetyl-CoA synthase
bifunctional enzyme
acetyl-CoA synthase/carbon monoxide dehydrogenase
-
bifunctional enzyme
ACS/CODH
Carbon dioxide/carbon monoxide oxidoreductase
-
-
-
-
Carbon monoxide dehydrogenase
-
-
-
-
carbon monoxide dehydrogenase-corrinoid enzyme complex
-
-
-
-
carbon monoxide dehydrogenase/acetyl-CoA synthase
-
bifunctional enzyme
Carbon monoxide oxidoreductase
-
-
-
-
Cdh
-
-
-
-
CO dehydrogenase
-
-
-
-
CO dehydrogenase/acetyl-CoA synthase
-
-
-
-
Co-DG
-
-
-
-
CODH
CODH/ACS
CODHACS
-
bifunctional enzyme, CODHACS is a macromolecular machine that catalyzes the last step of the Wood-Ljungdahl pathway of anaerobic carbon dioxide fixation
Dehydrogenase, carbon monoxide
-
-
-
-
ACS/CODH
-
bifunctional enzyme with ACS alpha subunits and CODH beta subunits
CODH
-
-
-
-
CODH
-
beta subunit of the bifunctional acetyl coenzyme A synthase/carbon monoxide dehydrogenase complex
CODH/ACS
-
bifunctional enzyme carbon monoxide dehydrogenase/acetyl-CoA synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
ping-pong mechanism
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
enzyme also catalyzes acetyl-CoA/CoA and acetyl-CoA/CO exchange reaction, enzyme has both CO-dehydrogenase and acetyl-CoA synthase activity
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
CO2/CO tunnel gating mechanism
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
mechanism, CO binding labilizes the hydroxyl bridging Ni and Fe and increases the nucleophilic tendency toward attacking Ni-bound carbonyl
-
CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+
CO and CO2 enter and exit the enzyme at the water channel along the betabeta subunit interface. CO either enters the enzyme and migrates through the tunnel before binding at the A-cluster, or it binds the A-cluster directly from solvent
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -
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
64972-88-9
-
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
acetyl-SCoA + CO
acetyl-SCoA + CO
-
acetyl-CoA/CO exchange reaction, 14C experiments prove that the enzyme can cleave both the carbon-carbon and carbon-sulfur bonds of acetyl-CoA as well as to store methyl, CO, and CoA fragments at the active site
-
r
acetyl-SCoA + CoASH
acetyl-SCoA + CoASH
-
acetyl-CoA/CoA exchange reaction
-
r
CO + H2O + cytochrome c3
CO2 + reduced cytochrome c3
-
cytochrome 3 from Desulfovibrio vulgaris
-
?
CO + H2O + oxidized cytochrome b
CO2 + reduced cytochrome b
-
membrane-bound b-type, native electron carrier
-
-
?
CO + H2O + oxidized cytochrome c3
CO2 + reduced cytochrome c3
-
Desulfovibrio vulgaris cytochrome c3
-
-
?
CO + H2O + oxidized flavodoxin
CO2 + reduced flavodoxin
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methylene blue
CO2 + reduced methylene blue
-
-
-
-
?
CO + H2O + oxidized rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
-
?
propionyl-SCoA + CoASH
propionyl-SCoA + CoASH
-
acetyl-CoA/CoA exchange reaction
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + electron acceptor
?
-
the enzyme is involved in the Wood pathway of acetyl-CoA synthesis
-
-
?
CO + H2O + electron acceptor
?
-
delivery of a low-potential electron to the CO-bound NiFe complex is the physiological function of the CO oxidation reaction catalyzed by the enzyme
-
-
?
CO + H2O + electron acceptor
?
-
the formation of acetyl-CoA from methyltetrahydrofolate requires several enzymes, including CO dehydrogenase
-
-
?
CO + H2O + electron acceptor
?
-
ferredoxin and a membrane-bound b-type cytochrome are considered to be the native electron carriers
-
-
?
CO + H2O + electron acceptor
?
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
the physiological role of the enzyme in acetyl-CoA synthesis is the reduction of CO2 to a bound CO, the physiological electron acceptor is not known and may be different in different organisms
-
-
?
CO + H2O + electron acceptor
?
-
key role of the enzyme in the synthesis of acetyl-CoA
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
active with ferredoxin obtained from Clostridium thermoaceticum, no activity with ferredoxin from spinach
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
r
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the exchange reaction between coenzyme A and acetyl-CoA
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the exchange reaction between coenzyme A and acetyl-CoA
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the exchange reaction between propionyl-CoA and CoA at 7% of the exchange with acetyl-CoA
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes at a low rate an exchange between CO2 and the carbonyl group of acetyl-CoA
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
no activity with FAD, NAD+ and NADP+
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes the synthesis of acetyl-CoA from methyl corrinoid, Co and CoASH
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes reversible decarbonylation of acetyl-CoA with retention of stereochemistry at the methyl group
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
ferredoxin I and II
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
ferredoxin from Clostridium pasteurianum is also a substrate
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
acetate biosynthesis pathway, catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
initial step of CO metabolism in acetogenic bacteria
-
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
?
additional information
?
-
-
pure enzyme has no hydrogenase or formate dehydrogenase activity
-
-
?
additional information
?
-
-
spinach ferredoxin, FAD, NAD+ and NADP+ are not reduced
-
-
?
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
CO + H2O + oxidized cytochrome b
CO2 + reduced cytochrome b
-
membrane-bound b-type, native electron carrier
-
-
?
CO + H2O + electron acceptor
?
-
the enzyme is involved in the Wood pathway of acetyl-CoA synthesis
-
-
?
CO + H2O + electron acceptor
?
-
delivery of a low-potential electron to the CO-bound NiFe complex is the physiological function of the CO oxidation reaction catalyzed by the enzyme
-
-
?
CO + H2O + electron acceptor
?
-
the formation of acetyl-CoA from methyltetrahydrofolate requires several enzymes, including CO dehydrogenase
-
-
?
CO + H2O + electron acceptor
?
-
ferredoxin and a membrane-bound b-type cytochrome are considered to be the native electron carriers
-
-
?
CO + H2O + electron acceptor
?
-
catalyzes the final step in the synthesis of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
the physiological role of the enzyme in acetyl-CoA synthesis is the reduction of CO2 to a bound CO, the physiological electron acceptor is not known and may be different in different organisms
-
-
?
CO + H2O + electron acceptor
?
-
key role of the enzyme in the synthesis of acetyl-CoA
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
acetate biosynthesis pathway, catalyzes an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
initial step of CO metabolism in acetogenic bacteria
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ni-Fe-S center
-
uses a Ni-Fe-S center called the C-cluster to reduce carbon dioxide to carbon monoxide and uses a second Ni-Fe-S center, called the A-cluster, to assemble acetyl-CoA from a methyl group, coenzyme A, and C-cluster-generated CO
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Ni2+
Nickel
Zinc
additional information
-
no oligomerization or activity in the presence of Co2+, Zn2+, and Cu2+, oligomerization but no exhibition of catalytic activity in the presence of Pd2+ and Pt2+
Iron
-
the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Iron
-
CO oxidation occurs at Ni- and FeS containing center C, electrons are transferred from cluster C via center B to external electron acceptors
Iron
-
the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
Iron
-
contains 11 mol of iron and 14 mol of acid-labile sulfur per mol of alphabeta dimer
Ni2+
-
contains Ni2+-activated alpha subunits, Ni2+ is required for activity and oligomerization
Nickel
-
the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Nickel
-
both CO and CoASH bind near the nickel site, nickel may therefore be the active metal center for C-C bond formation
Nickel
-
the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Zinc
-
the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM, inactivates CO/acetyl-CoA exchange activity completely but has no effect on CO oxidation
KCN
-
CO reverses cyanide inhibition, but promotes reaction with methyl iodide
CN-
-
dithionite slows the inhibition, but cannot reactivate the enzyme
additional information
-
not inhibited by propyl iodide, methyl iodide, carbon tetrachloride, EDTA or nitrilotriacetate
-
additional information
-
not affected by propyl iodide, methyl iodide, carbon tetrachloride,or metal chelators
-
additional information
-
phenylglyoxal, methylglyoxal, butanedione, mersalyl acid, methyl iodide, 5,5'-dithiobis (2-nitrobenzoate) and sodium dithionite inhibits the exchange reaction between CO and acetyl-CoA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Nickel
-
Ni-activated alpha subunit rapidly and reversibly accepts a methyl group
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
42000/min/Ni, substrate methyl viologen
-
additional information
additional information
-
pH 5.3, 50°C, activity of CO oxidation to CO2, ferredoxin II as electron carrier, turnover number is approximately 780 mol/mol of CO dehydrogenase
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
pivaloylpantetheine-SH
-
inhibition of CO/acetyl-CoA exchange reaction
0.4
CO
-
noncompetitive inhibition of the acetyl-CoA exchange reaction
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
-
acetyl-CoA/CoA exchange reaction at pH 6.0 and 45°C, CO in the gas phase replaced by N2
7
-
acetyl-CoA/CoA exchange reaction at pH 6.0 and 45°C, 100% CO in the gas phase
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CODH/ACS subunit beta; formerly Clostridium thermoaceticum strain ATCC 39073
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). DCMB_MOOTH
674
0
72924
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
71000
73000
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
78000
82000
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
71000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
78000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
tetramer
hexamer
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A110C
A219F
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
A222L
A265M
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, little synthesis of acetyl-CoA
A578C
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
F70W
-
mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
H113A
-
44% of wild type activity, in presence of imidazole, 45% of wild type activity
H116A
-
6% of wild type activity, in presence of imidazole, 3% of wild type activity
L215F
-
mutant designed to block tunnel between Ni-Fe-S active site clusters, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
N101Q
-
mutant designed to block region that connects the CO tunnel at the betabeta interface with a water channel, little enzymic activity. Metal clusters are properly assembled, impaired ability of CO to migrate through the tunnel
A110C
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, no synthesis of acetyl-CoA
A110C
-
alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation
A222L
-
mutation within tunnel region of alpha subunit, absence of strong cooperative inhibition of CO, no synthesis of acetyl-CoA
A222L
-
alpha subunit mutant enzyme showing electron paramagnetic resonance spectrum after Ni-activation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
-
purification can be done at 25°C without loss of activity, heating for 30 min at 67°C leads to apparent loss, heating for only a few min at 70°C activates the enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
addition of the enzyme to an aerobic buffer, 50 mM Tris/HCl, pH 7.6 results in a 98% loss of activity within 15 min, presence of CO has no apparent effect on the stability of the enzyme
-
390452
enzymatic activity is destroyed by air, a low amount of activity still is present after 2 h exposure to air
-
390454
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 5°C, 50 mM Tris/HCl, pH 7.5, 2 mM sodium dithionite, 0.2 mM methyl viologen, 50% v/v glycerol, stable for more than 1 month
-
-20°C, stored frozen in an oxygen-free atmosphere in buffer containing glycerol and 2 mM dithionite, not stable for more than 1 month
-
5°C, stored in an oxygen-free atmosphere in buffer containing glycerol and 2 mM dithionite, not stable for more than 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fuchs, G.
CO2 fixation in acetogenic bacteria: variations on a theme
FEMS Microbiol. Rev.
39
181-213
1986
Acetobacterium woodii, Clostridium pasteurianum, Moorella thermoacetica
-
Ragsdale, S.W.; Clark, J.E.; Ljungdahl, L.G.; Lundie, L.L.; Drake, H.L.
Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein
J. Biol. Chem.
258
2364-2369
1983
Moorella thermoacetica
Diekert, G.; Ritter, M.
Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum
FEBS Lett.
151
141-144
1983
Moorella thermoacetica
-
Drake, H.L.; Hu, S.I.; Wood, H.G.
Purification of carbon monoxide dehydrogenase, a nickel enzyme from Clostridium thermoaceticum
J. Biol. Chem.
255
7174-7180
1980
Moorella thermoacetica
Lebertz, H.; Simon, H.; Courtney, L.F.; Benkovic, S.J.; Zydowsky, L.D.; Lee, K.; Floss, H.G.
Stereochemistry of acetic acid formation from 5-methyltetrahydrofolate by Clostridium thermoaceticum
J. Am. Chem. Soc.
109
3173-3174
1987
Moorella thermoacetica
-
Wood, H.G.; Ragsdale, S.W.; Pezacka, E.
The acetyl-CoA pathway of autotrophic growth
FEMS Microbiol. Rev.
39
345-362
1986
Acetobacterium woodii, Moorella thermoacetica, Methanosarcina barkeri, Methanothermobacter thermautotrophicus
-
Ragsdale, S.W.; Wood, H.G.
Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis
J. Biol. Chem.
260
3970-3977
1985
Moorella thermoacetica
Raybuck, S.A.; Bastian, N.R.; Zydowsky, L.D.; Kobayashi, K.; Floss, H.G.; Orme-Johnson, W.H.; Walsh, C.T.
Nickel-containing CO dehydrogenase catalyzes reversible decarbonylation of acetyl-CoA with retention of stereochemistry at the methyl group
J. Am. Chem. Soc.
109
3171-3173
1987
Moorella thermoacetica
-
Seravalli, J.; Kumar, M.; Lu, W.P.; Ragsdale, S.W.
Mechanism of CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by anions
Biochemistry
34
7879-7888
1995
Moorella thermoacetica
Shin, W.; Lindahl, P.A.
Function and CO binding properties of the NiFe complex in carbon monoxide dehydrogenase from Clostridium thermoaceticum
Biochemistry
31
12870-12875
1992
Moorella thermoacetica
Anderson, M.E.; Lindahl, P.A.
Organization of clusters and internal electron pathways in CO dehydrogenase from Clostridium thermoaceticum: relevance to the mechanism of catalysis and cyanide inhibition
Biochemistry
33
8702-8711
1994
Moorella thermoacetica
Raybuck, S.A.; Bastian, N.R.; Orme-Johnson, W.H.; Walsh, C.T.
Kinetic characterization of the carbon monoxide-acetyl-CoA (carbonyl group) exchange activity of the acetyl-CoA synthesizing CO dehydrogenase from Clostridium thermoaceticum
Biochemistry
27
7698-7702
1988
Moorella thermoacetica
Ramer, S.E.; Raybuck, S.A.; Orme-Johnson, W.H.; Walsh, C.T.
Kinetic characterization of the [3'-32P]coenzyme A/acetyl coenzyme A exchange catalyzed ba a three-subunit form of the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum
Biochemistry
28
4675-4680
1989
Moorella thermoacetica
Lu, W.P.; Ragsdale, S.W.
Reductive activation of the coenzyme A/acetyl-CoA isotopic exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by nitrous oxide and carbon monoxide
J. Biol. Chem.
266
3554-3564
1991
Moorella thermoacetica
Anderson, M.E.; DeRose, V.J.; Hoffman, B.M.; Lindahl, P.A.
Identification of a cyanide binding site in CO dehydrogenase from Clostridium thermoaceticum using EPR and ENDOR spectroscopies
J. Am. Chem. Soc.
115
12204-12205
1993
Moorella thermoacetica
-
Xia, J.; Sinclair, J.F.; Baldwin, T.O.; Lindahl, P.A.
Carbon monoxide dehydrogenase from Clostridium thermoaceticum: quaternary structure, stoichiometry of its SDS-induced dissociation, and characterization of the faster-migrating form
Biochemistry
35
1965-1971
1996
Moorella thermoacetica
Seravalli, J.; Kumar, M.; Lu, W.P.; Ragsdale, S.W.
Mechanism of carbon monoxide oxidation by the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum: Kinetic characterization of the intermediates
Biochemistry
36
11241-11251
1997
Moorella thermoacetica
Kim, E.J.; Feng, J.; Bramlett, M.R.; Lindahl, P.A.
Evidence for a proton transfer network and a required persulfide-bond-forming cysteine residue in Ni-containing carbon monoxide dehydrogenases
Biochemistry
43
5728-5734
2004
Moorella thermoacetica
Feng, J.; Lindahl, P.A.
Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases
J. Am. Chem. Soc.
126
9094-9100
2004
Moorella thermoacetica, Rhodospirillum rubrum
Tan, X.; Loke, H.K.; Fitch, S.; Lindahl, P.A.
The tunnel of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase regulates delivery of CO to the active site
J. Am. Chem. Soc.
127
5833-5839
2005
Moorella thermoacetica
Volbeda, A.; Fontecilla-Camps, J.C.
Crystallographic evidence for a CO/CO(2) tunnel gating mechanism in the bifunctional carbon monoxide dehydrogenase/acetyl coenzyme A synthase from Moorella thermoacetica
J. Biol. Inorg. Chem.
9
525-532
2004
Moorella thermoacetica
Tan, X.; Volbeda, A.; Fontecilla-Camps, J.C.; Lindahl, P.A.
Function of the tunnel in acetylcoenzyme A synthase/carbon monoxide dehydrogenase
J. Biol. Inorg. Chem.
11
371-378
2006
Moorella thermoacetica
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
Tan, X.; Kagiampakis, I.; Surovtsev, I.V.; Demeler, B.; Lindahl, P.A.
Nickel-dependent oligomerization of the alpha subunit of acetyl-coenzyme A synthase/carbon monoxide dehydrogenase
Biochemistry
46
11606-11613
2007
Moorella thermoacetica
Doukov, T.I.; Blasiak, L.C.; Seravalli, J.; Ragsdale, S.W.; Drennan, C.L.
Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
Biochemistry
47
3474-3483
2008
Moorella thermoacetica
Seravalli, J.; Ragsdale, S.W.
Pulse-chase studies of the synthesis of acetyl-CoA by carbon monoxide dehydrogenase/acetyl-CoA synthase: evidence for a random mechanism of methyl and carbonyl addition
J. Biol. Chem.
283
8384-8394
2008
Moorella thermoacetica, Methanosarcina thermophila
Tan, X.; Lindahl, P.A.
Tunnel mutagenesis and Ni-dependent reduction and methylation of the alpha subunit of acetyl coenzyme A synthase/carbon monoxide dehydrogenase
J. Biol. Inorg. Chem.
13
771-778
2008
Moorella thermoacetica
EXTERNAL LINKS (specific for EC-Number 1.2.7.4)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
