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Information on EC 1.2.2.4 - carbon-monoxide dehydrogenase (cytochrome b-561) for references in articles please use BRENDA:EC1.2.2.4
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EC Tree
IUBMB Comments Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
co dehydrogenase, carbon monoxide dehydrogenase,
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Carbon dioxide/carbon monoxide oxidoreductase
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Carbon monoxide dehydrogenase
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Carbon monoxide oxidoreductase
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carbon monoxide, water:cytochrome b-561 oxidoreductase
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carbon-monoxide oxygenase (cytochrome b-561)
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chromaffin granule cytochrome b-561
Dehydrogenase, carbon monoxide
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duodenal cytochrome b-561
lysosomal cytochrome b-561
chromaffin granule cytochrome b-561
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chromaffin granule cytochrome b-561
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chromaffin granule cytochrome b-561
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CO dehydrogenase
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duodenal cytochrome b-561
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duodenal cytochrome b-561
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duodenal cytochrome b-561
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lysosomal cytochrome b-561
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lysosomal cytochrome b-561
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lysosomal cytochrome b-561
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CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
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CO + H2O + 2 ferricytochrome b-561 = CO2 + 2 H+ + 2 ferrocytochrome b-561
mechanism, necessity of S-selanyl-cysteine for catalysis
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carbon monoxide,water:cytochrome b-561 oxidoreductase
Contains molybdopterin cytosine dinucleotide, FAD and [2Fe-2S]-clusters. Oxygen, methylene blue and iodonitrotetrazolium chloride can act as nonphysiological electron acceptors.
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
Fe3+-EDTA + H2O + ferrocytochrome b-561
Fe2+-EDTA + H+ + ferricytochrome b-561
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potassium ferricyanide + H2O + ferrocytochrome b-561
potassium ferrocyanide + H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + 2 H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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CO + H2O + ferrocytochrome b-561
CO2 + H+ + ferricytochrome b-561
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the only enzyme involved in CO oxidation by carboxydotrophic bacteria
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FAD
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contains 2 mol of non-covalently bound FAD per mol of enzyme
FAD
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contains 2 mol of non-covalently bound FAD per mol of enzyme
FAD
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contains 2 mol of non-covalently bound FAD per mol of enzyme
FAD
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2.2 mol per mol of enzyme dimer
molybdenum cofactor
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the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
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the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
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the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
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the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
molybdenum cofactor
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the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
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Mo5+
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1.9 mol per mol of enzyme dimer, a 1:1 mononuclear complex of molybdopterin-cytosine dinucleotide and the Mo ion
Mo6+
functions in the proper orientation of the catalytically active residues C385 and E757, crystalization data
[2Fe-2S]-center
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6.9 mol per mol of enzyme dimer, type I and type II [2Fe-2S]-centers
additional information
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the reconstitution reaction of the solubilized enzyme with depleted membranes requires cations with effectiveness that increases with increasing ionic charge: Li+, Mg2+, Mn2+, Cr3+, La3+
Iron
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enzyme contains 8 mol of Fe and 8 mol of acid-labile sulfide groups per mol of enzyme
Iron
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enzyme contains 2 different types of Fe2S2 centers; enzyme contains 8 mol of Fe and 8 mol of acid-labile sulfide groups per mol of enzyme
Iron
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enzyme contains 2 different types of Fe2S2 centers; enzyme contains 8 mol of Fe and 8 mol of acid-labile sulfide groups per mol of enzyme
Molybdenum
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enzyme contains Mo; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
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enzyme contains 2 mol of Mo per mol of enzyme; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
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enzyme contains 2 mol of Mo per mol of enzyme; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
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the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
Molybdenum
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enzyme contains Mo; the enzyme contains a molybdenum cofactor, which is non-covalently bound to the enzyme. Bactopterin is the organic portion of the molybdenum cofactor
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Starvation
Characterization of the Photosynthetic Apparatus and Proteome of Roseobacter denitrificans.
Tuberculosis
In vitro and in vivo studies of a rapid and selective breath test for tuberculosis based upon mycobacterial CO dehydrogenase.
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0.053
CO
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
carbon monoxide dehydrogenase large chain
Swissprot
brenda
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brenda
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the portion of enzyme localized in the cytoplasm is low during exponential growth and high in stationary cells
brenda
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a weakly-bound pool and a tightly-bound pool of the enzyme
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brenda
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attached to the inner surface
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brenda
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A3RYZ1_RALSL
194
0
20965
TrEMBL
A0A1B4WV72_9PSED
181
4
19990
TrEMBL
G9FZ04_ONCGO
150
3
16874
TrEMBL
I1Y6Y1_9SYLV
205
5
22770
TrEMBL
G9FZ10_ONCGO
150
3
16968
TrEMBL
Q3KAW8_PSEPF
Pseudomonas fluorescens (strain Pf0-1)
183
4
20365
TrEMBL
I1Y6Y3_9SYLV
213
5
23691
TrEMBL
I1Y6X9_9SYLV
205
5
22770
TrEMBL
A3RYZ4_RALSL
175
0
18401
TrEMBL
C9Y525_CROTZ
Cronobacter turicensis (strain DSM 18703 / LMG 23827 / z3032)
193
4
22094
TrEMBL
G9FZ11_ONCKE
150
3
16961
TrEMBL
K9NH87_9PSED
181
4
19954
TrEMBL
I1Y6Y4_9SYLV
213
5
23657
TrEMBL
F1DSD7_CANLU
32
1
3581
TrEMBL
G9FZ07_ONCGO
150
3
16948
TrEMBL
I1Y6X8_9SYLV
205
5
22770
TrEMBL
G9FZ02_ONCGO
150
3
17006
TrEMBL
G9FZ05_ONCGO
150
3
16907
TrEMBL
G9FZ03_ONCGO
150
3
16934
TrEMBL
DCML_HYDPS
803
0
87229
Swiss-Prot
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14000
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3 * 14000 + 3 * 28000 + 3 * 85000
17750
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x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
17800
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
27000
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deduced from sequence, Western blot
27800
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deduced from sequence, Western blot
28000
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3 * 14000 + 3 * 28000 + 3 * 85000
30200
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
30700
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x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
31500
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deduced from sequence, Western blot
85000
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3 * 14000 + 3 * 28000 + 3 * 85000
87200
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x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
88700
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
140000
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2 * 140000, SDS-PAGE
230000
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sucrose density gradient centrifugation, sedimentation equilibrium experiments, gel filtration
17000
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2 * 17000 + 2 * 33000 + 2 * 70000
17000
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2 * 17000 + 2 * 33000 + 2 * 70000
33000
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2 * 17000 + 2 * 33000 + 2 * 70000
33000
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2 * 17000 + 2 * 33000 + 2 * 70000
70000
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2 * 17000 + 2 * 33000 + 2 * 70000
70000
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2 * 17000 + 2 * 33000 + 2 * 70000
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x * 87200, molybdopterin binding subunit L, + x * 30700, FAD-binding subunit M, + x * 17750, subunit S with two [2Fe-2S]-center binding sites, deduced from gene sequence
dimer
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2 * 140000, SDS-PAGE
heterohexamer
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2 * 88700, molybdoprotein L, + 2 * 30200, flacoprotein M, + 2 * 17800 iron-sulfur-protein S, crystallization data
nonamer
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3 * 14000 + 3 * 28000 + 3 * 85000
hexamer
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2 * 17000 + 2 * 33000 + 2 * 70000
hexamer
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2 * 17000 + 2 * 33000 + 2 * 70000
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additional information
R384 has a gamma-hydroxy modification, C385 carries the catalytically essential S-selanyl-group
molybdoironflavoprotein
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molybdoironflavoprotein
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molybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotide and S-selanylcysteine at active site
molybdoironflavoprotein
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D38A
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similar to wild-type, mutation in the transmembrane domain
E177A
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similar to wild-type, mutation in the electron donating site
E196A
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23% activity, mutation in the electron donating site
F44A
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45% activity, mutation in the transmembrane domain
H105A
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similar to wild-type, mutation in the electron donating site
H112A
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similar to wild-type, mutation in the electron donating site
H117A
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inactive, residues involved in heme-binding
H156A
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inactive, residues involved in heme-binding
H47A
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inactive, residues involved in heme-binding
H83A
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inactive, residues involved in heme-binding
M51A
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similar to wild-type, mutation in the transmembrane domain
N106A
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similar to wild-type, mutation in the electron donating site
P48A
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similar to wild-type, mutation in the transmembrane domain
Q131A
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45% activity, mutation in the transmembrane domain
R149A
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25% activity, residue at the electron-accepting site of the protein
R67A
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incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
S115A
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50% activity, mutation in the electron donating site
S118A
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similar to wild-type, mutation in the electron donating site
W119A
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17% activity, mutation in the electron donating site
Y190A
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similar to wild-type, mutation in the electron donating site
Y66A
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incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
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expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Chromaffin granule cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Duodenal cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Lysosomal cytochrome b-561 could partially restore the wild-type phenotype
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genes for subunits L,M,S
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Jacobitz, S.; Meyer, O.
Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities
J. Bacteriol.
171
6294-6299
1989
Oligotropha carboxidovorans
brenda
Meyer, O.; Jacobitz, S.; Kruger, B.
Biochemistry, and physiology of aerobic carbon monoxide-utilizing bacteria
FEMS Microbiol. Rev.
39
161-179
1986
Hydrogenibacillus schlegelii, Hydrogenophaga pseudoflava, Oligotropha carboxidovorans, Pseudomonas carboxydohydrogena, Pseudomonas thermocarboxydovorans
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brenda
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
Oligotropha carboxidovorans
brenda
Kang, B.S.; Kim, Y.M.
Cloning and molecular characterization of the genes for carbon monoxide dehydrogenase and localization of molybdopterin, flavin adenine dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga pseudoflava
J. Bacteriol.
181
5581-5590
1999
Hydrogenophaga pseudoflava
brenda
Hanzelmann, P.; Hofmann, B.; Meisen, S.; Meyer, O.
The redox centers in the molybdo iron-sulfur flavoprotein CO dehydrogenase from the thermophilic carboxidotrophic bacterium Pseudomonas thermocarboxydovorans
FEMS Microbiol. Lett.
176
139-145
1999
Pseudomonas thermocarboxydovorans
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brenda
Hanzelmann, P.; Dobbek, H.; Gremer, L.; Huber, R.; Meyer, O.
The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase
J. Mol. Biol.
301
1221-1235
2000
Hydrogenophaga pseudoflava, Hydrogenophaga pseudoflava (P19913)
brenda
Su, D.; Asard, H.
Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases
FEBS J.
273
3722-3734
2006
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Swingley, W.D.; Sadekar, S.; Mastrian, S.D.; Matthies, H.J.; Hao J.; Ramos, H.; Acharya, C.R.; Conrad, A.L.; Taylor, H.L.; Dejesa, L.C.; Shah, M.K.; O'huallachain, M.E.; Lince, M.T.; Blankenship, R.E.; Beatty, J.T.; Touchman, J.W.
The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism
J. Bacteriol.
189
683-690
2007
Roseobacter denitrificans OCh 114
brenda
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1.2.2.4 carbon-monoxide dehydrogenase (cytochrome b-561)
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