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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 + ferredoxin
?
-
ferredoxin is the direct electron acceptor, the carbon-monoxide dehydrogenase complex reduces a ferredoxin which, together with membranes and associated hydrogenase, reconstitutes a CO-oxidizing:H2-evolving system
-
-
?
CO + H2O
CO2 + H2
-
-
-
?
CO + H2O + 1,1'-trimethylene-4,4'-dimethyl-2,2'dipyridylium dibromide
CO2 + reduced 1,1'-trimethylene-4,4'-dimethyl-2,2'dipyridylium dibromide
-
-
-
?
CO + H2O + 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO + H2O + acceptor
CO2 + reduced acceptor
CO + H2O + acceptor
CO2 + reduced acceptor + H+
-
-
-
-
?
CO + H2O + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
?
CO + H2O + coenzyme F420
CO2 + reduced coenzyme F420
CO + H2O + cytochrome b
CO2 + reduced cytochrome b
-
-
-
?
CO + H2O + cytochrome c3
CO2 + reduced cytochrome c3
-
cytochrome 3 from Desulfovibrio vulgaris
-
?
CO + H2O + electron acceptor
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
-
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 + FAD
CO2 + FADH2
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
CO + H2O + flavodoxin
CO2 + reduced flavodoxin
-
-
-
?
CO + H2O + FMN
CO2 + FMNH2
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
CO + H2O + methyl viologen
CO2 + reduced methyl viologen + H+
CO + H2O + methylene blue
CO2 + reduced methylene blue
CO + H2O + methylene blue
CO2 + reduced methylene blue + H2
-
-
-
-
?
CO + H2O + NAD+
CO2 + NADH + H+
CO + H2O + NADP+
CO2 + NADPH + H+
CO + H2O + oxidized 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
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 ferredoxin
CO2 + reduced ferredoxin
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
CO + H2O + oxidized flavodoxin
CO2 + reduced flavodoxin
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen + H+
CO + H2O + oxidized methylene blue
CO2 + reduced methylene blue
-
-
-
-
?
CO + H2O + oxidized phenazine methosulfate
CO2 + reduced phenazine methosulfate
-
-
-
-
?
CO + H2O + oxidized rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
-
?
CO + H2O + oxidized viologen
CO2 + reduced viologen
-
-
-
-
?
CO + H2O + phenazine methosulfate
CO2 + reduced phenazine methosulfate
-
-
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
H2 + reduced methyl viologen
methyl viologen
-
-
-
-
r
propionyl-SCoA + CoASH
propionyl-SCoA + CoASH
-
acetyl-CoA/CoA exchange reaction
-
r
tetrahydrosarcinapterin + acetyl-SCoA + H2O
methyltetrahydrosarcinapterin + CO2 + CoASH
trichloroethylene + ?
cis-dichloroethylene + trans-dichlororethylene + 1,1-dichloroethylene + vinyl chloride + ethylene
-
-
-
?
additional information
?
-
CO + H2O + 2,3,5-triphenyltetrazolium chloride

CO2 + reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
?
CO + H2O + 2,3,5-triphenyltetrazolium chloride
CO2 + reduced 2,3,5-triphenyltetrazolium chloride
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride

CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
Mycobacterium tuberculosis TMC 326 / H37Ra-INH-R / ATCC 35835
-
-
-
-
?
CO + H2O + 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + acceptor

CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
Q7X0G5;
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
?
CO + H2O + coenzyme F420

CO2 + reduced coenzyme F420
-
1.5% of the activity with methyl viologen
-
?
CO + H2O + coenzyme F420
CO2 + reduced coenzyme F420
-
-
-
?
CO + H2O + electron acceptor

?
-
-
-
-
?
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 enzyme in C1-pathway of acetyl-CoA degradation
-
-
?
CO + H2O + electron acceptor
?
Autotrophic methanogenic bacterium
-
the enzyme is required for autotrophic CO2 fixation in methanogens, the enzyme is also involved in methanogenesis from acetate, not required for methanogenesis
-
-
?
CO + H2O + electron acceptor
?
-
the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the methylation of tetrahydrosarcinapterin in a reaction involving net cleavage of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
enzyme may also be involved in the formation of acetyl-CoA from methanol in methanogens
-
-
?
CO + H2O + electron acceptor
?
-
extensive role of the enzyme in the acetyl-CoA pathway, it is proposed that the enzyme serves as the CO, CH3, SCoA acceptor and catalyzes the final steps of the synthesis of acetyl-CoA
-
-
?
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
?
-
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 + FAD

CO2 + FADH2
-
-
-
?
CO + H2O + FAD
CO2 + FADH2
-
0.3% of the activity with methyl viologen
-
?
CO + H2O + FAD
CO2 + FADH2
-
-
-
?
CO + H2O + FAD
CO2 + FADH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + FAD
CO2 + FADH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + ferredoxin

CO2 + reduced ferredoxin
-
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
-
-
?
CO + H2O + ferredoxin
CO2 + reduced ferredoxin
-
active with ferredoxin obtained from Clostridium thermoaceticum, no activity with ferredoxin from spinach
-
?
CO + H2O + FMN

CO2 + FAD
-
-
-
-
?
CO + H2O + FMN
CO2 + FAD
-
-
-
-
?
CO + H2O + FMN

CO2 + FMNH2
-
-
-
?
CO + H2O + FMN
CO2 + FMNH2
-
0.6% of the activity with methyl viologen
-
?
CO + H2O + FMN
CO2 + FMNH2
-
-
-
?
CO + H2O + FMN
CO2 + FMNH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + FMN
CO2 + FMNH2
-
at 15% of the specific activity compared to methyl viologen
-
-
?
CO + H2O + FMN
CO2 + FMNH2
-
-
-
?
CO + H2O + FMN
CO2 + FMNH2
-
-
-
?
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 an exchange reaction between CO and the carbonyl group of acetyl-CoA
-
?
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
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
optimal concentration of CO 5% in headspace
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
no activity with NAD+ and NADP+
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
the enzyme fails to reduce NAD+, NADP+, or 8-hydroxy-5-deazaflavin cofactor 420
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
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 + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + methyl viologen

CO2 + reduced methyl viologen + H+
-
-
-
-
?
CO + H2O + methyl viologen
CO2 + reduced methyl viologen + H+
-
-
-
-
?
CO + H2O + methylene blue

CO2 + reduced methylene blue
-
-
-
?
CO + H2O + methylene blue
CO2 + reduced methylene blue
-
-
-
?
CO + H2O + methylene blue
CO2 + reduced methylene blue
-
-
-
?
CO + H2O + NAD+

CO2 + NADH + H+
-
the specific activity is increased by approximately 20% with NAD+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + NAD+
CO2 + NADH + H+
-
the specific activity is increased by approximately 20% with NAD+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + NADP+

CO2 + NADPH + H+
-
the specific activity is increased by approximately 20% with NADP+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + NADP+
CO2 + NADPH + H+
-
the specific activity is increased by approximately 20% with NADP+ as the electron acceptor compared to methyl viologen
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride

CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
-
-
-
-
?
CO + H2O + oxidized 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
CO2 + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-2H-tetrazolium chloride
D5G1Y2; D5G1Y0; D5G1Y1;
-
-
-
?
CO + H2O + oxidized ferredoxin

CO2 + reduced ferredoxin
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
may participate in methanogenesis by cleavage of acetate, reverse of the reaction in acetate biosynthesis
-
-
?
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 + oxidized ferredoxin

CO2 + reduced ferredoxin + H+
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
-
-
-
-
?
CO + H2O + oxidized flavodoxin

CO2 + reduced flavodoxin
-
-
-
-
?
CO + H2O + oxidized flavodoxin
CO2 + reduced flavodoxin
-
-
-
-
?
CO + H2O + oxidized methyl viologen

CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
no enzyme with cofactor F420
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
no enzyme with cofactor F420
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
CO + H2O + oxidized methyl viologen

CO2 + reduced methyl viologen + H+
-
-
-
-
?
CO + H2O + oxidized methyl viologen
CO2 + reduced methyl viologen + H+
-
-
-
-
?
CO + H2O + rubredoxin

CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
?
CO + H2O + rubredoxin
CO2 + reduced rubredoxin
-
most efficient electron acceptor
-
?
tetrahydrosarcinapterin + acetyl-SCoA + H2O

methyltetrahydrosarcinapterin + CO2 + CoASH
-
-
-
-
tetrahydrosarcinapterin + acetyl-SCoA + H2O
methyltetrahydrosarcinapterin + CO2 + CoASH
-
carbon monoxide dehydrogenase-corrinoid enzyme complex, enzyme complex functions in synthesis of acetyl-CoA
-
r
additional information

?
-
-
enzyme fails to reduce NAD+, NADP+ or the 8-hydroxy-5-deazaflavin factor F420
-
-
-
additional information
?
-
-
pure enzyme has no hydrogenase or formate dehydrogenase activity
-
-
-
additional information
?
-
-
spinach ferredoxin, FAD, NAD+ and NADP+ are not reduced
-
-
-
additional information
?
-
-
Thermacetogenium phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CO + ferredoxin
?
-
ferredoxin is the direct electron acceptor, the carbon-monoxide dehydrogenase complex reduces a ferredoxin which, together with membranes and associated hydrogenase, reconstitutes a CO-oxidizing:H2-evolving system
-
-
?
CO + H2O
CO2 + H2
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
CO + H2O + acceptor
CO2 + reduced acceptor + H+
-
-
-
-
?
CO + H2O + electron acceptor
?
CO + H2O + electron acceptor
CO2 + reduced electron acceptor
-
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 + oxidized cytochrome b
CO2 + reduced cytochrome b
-
membrane-bound b-type, native electron carrier
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
additional information
?
-
-
Thermacetogenium phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus
-
-
-
CO + H2O + acceptor

CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
r
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
Q9F8A8
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
P27989
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
D5G1Y2 and D5G1Y0 and D5G1Y1
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
-
-
-
-
?
CO + H2O + acceptor
CO2 + reduced acceptor
P19919 and P19920 and P19921
-
-
-
?
CO + H2O + electron acceptor

?
-
-
-
-
?
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 enzyme in C1-pathway of acetyl-CoA degradation
-
-
?
CO + H2O + electron acceptor
?
Autotrophic methanogenic bacterium
-
the enzyme is required for autotrophic CO2 fixation in methanogens, the enzyme is also involved in methanogenesis from acetate, not required for methanogenesis
-
-
?
CO + H2O + electron acceptor
?
-
the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the methylation of tetrahydrosarcinapterin in a reaction involving net cleavage of acetyl-CoA
-
-
?
CO + H2O + electron acceptor
?
-
enzyme may also be involved in the formation of acetyl-CoA from methanol in methanogens
-
-
?
CO + H2O + electron acceptor
?
-
extensive role of the enzyme in the acetyl-CoA pathway, it is proposed that the enzyme serves as the CO, CH3, SCoA acceptor and catalyzes the final steps of the synthesis of acetyl-CoA
-
-
?
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
?
-
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
-
may participate in methanogenesis by cleavage of acetate, reverse of the reaction in acetate biosynthesis
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin
-
-
-
-
?
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 + oxidized ferredoxin

CO2 + reduced ferredoxin + H+
-
-
-
-
?
CO + H2O + oxidized ferredoxin
CO2 + reduced ferredoxin + H+
-
-
-
-
?
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4Fe-4S cluster
-
core extrusion experiments indicate 6 [4Fe-4S] clusters per tetramer, and electron paramagnetic resonance spectroscopy detects at least one of these clusters, in the reduced form
Co2+
-
the multifunctional enzyme complex contains Co2+
Fe-S center
-
the multifunctional enzyme complex contains iron-sulfur centers
S2-
-
contains a [NiFe4S5] center called cluster C
Zn2+
-
the multifunctional enzyme complex contains Zn2+
[2Fe-2S]-center
-
the small subunit contains two [2Fe-2S] centers
copper

-
dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
copper
-
contains copper, essential for activity
copper
-
synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
Cu2+

-
the enzyme contains copper
Cu2+
-
the native enzyme contains copper in the active site
Fe2+

-
contains a NiFe center, called C-cluster
Fe2+
-
contains 9 Fe+ per monomer
Fe2+
-
contains one Ni-4Fe-5S cluster
Fe2+
-
contains a [NiFe4S5] center called cluster C; Ni-, Fe-, and S-containing metal center called cluster C
Fe2+
-
CODHII contains iron, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Fe2+
-
contains iron in form of Ni4Fe-4S clusters
Fe2+
-
tightly bound by the enzyme
Fe2+
-
contains a NiFe center, called C-cluster
Fe2+
-
the enzyme contains iron
Fe2+
-
contains a NiFe center, called C-cluster
Iron

-
the alphabeta dimer contains approximately 9-11 mol of iron and 12-14 mol of acid-labile sulfur per mol of dimer
Iron
-
61.5 mol nonheme iron per mol of complex
Iron
-
[Ni-4Fe-4S] cluster or [Ni-4Fe-5S] cluster
Iron
-
0.58, 0.67 and 1.96 atoms of iron per mol of large, medium- and small subunit, two iron-sulfur centers are associated with the small subunit
Iron
-
contains 15.6 mol of iron per mol of alpha2beta oligomer
Iron
-
contains 25 mol of Fe2+ and 20 mol of S2- per mol of tetramer, the enzyme contains 2 (4Fe-4S)+ clusters
Iron
-
CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
Iron
-
enzyme contains 3 iron containing centers: center A contains nickel and iron and is suggested to be the acetyl-CoA cleavage site, center B is a [4Fe-4S]2+/1+ center, center C is a fast relaxing center
Iron
-
CO oxidation occurs at Ni- and FeS containing center C, electrons are transferred from cluster C via center B to external electron acceptors; 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
Iron
-
the NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Iron
-
enzyme form I contains 7 iron and 6 sulfur per monomer; enzyme form II contains 9 iron and 8 sulfur per monomer
Iron
-
the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [Fe4S4]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor
Iron
-
enzyme utilizes three types of Fe-S clusters: a [Ni4Fe5S] C-cluster catalyzing the CO oxidation, and 2 distinct [4Fe4S] electron-transfer sites called clusters B and D
Iron
-
wild-type, 8.97 mol per mol of enzyme
Molybdenum

-
2.29 mol/mol enzyme
Molybdenum
-
molybdopterin-cytosine dinucleotide cofactor is composed of a molybdenum ion with 2 oxo- and 1 hydroxoligand complexed by the enedithiolene group of molybdopterin
Molybdenum
-
dinuclear heterometal [CuSMo(=O)OH] cluster in the active site
Molybdenum
-
the enzyme contains molybdenum
Molybdenum
-
contains molybdenum, essential for activity
Molybdenum
-
synthesis and characterization of dinuclear Mo-Cu complexes relevant to the active site of MoCu-enzyme by X-ray diffraction studies and by reactivity
Ni2+

-
contains a NiFe center, called C-cluster
Ni2+
-
contains 0.1 Ni2+ per monomer
Ni2+
-
contains one Ni-4Fe-5S cluster
Ni2+
-
contains a [NiFe4S5] center called cluster C; Ni-, Fe-, and S-containing metal center called cluster C
Ni2+
-
CODHII contains nickel, the active site of CODH contains a [NiFe4S4OHx] cluster known as C-cluster
Ni2+
-
contains nickel in form of Ni4Fe-4S clusters
Ni2+
-
tightly bound by the enzyme
Ni2+
-
Ni is tightly bound to the enzyme and is not removed by anaerobic dialysis or gel permeation
Ni2+
-
the multifunctional enzyme complex contains Ni2+
Ni2+
-
contains a NiFe center, called C-cluster
Ni2+
-
contains Ni2+-activated alpha subunits, Ni2+ is required for activity and oligomerization
Ni2+
-
contains a NiFe center, called C-cluster
Nickel

-
the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
-
carbon monoxide dehydrogenase II, enzyme contains 5 metal clusters, a [Ni-4Fe-5S] cluster appears to be the active site of CO oxidation
Nickel
-
3 mol per mol of complex
Nickel
-
[Ni-4Fe-4S] cluster or [Ni-4Fe-5S] cluster
Nickel
-
contains nickel in a NiFe3S4 cluster
Nickel
-
contains 2 g-atoms of nickel per mol of enzyme
Nickel
-
contains 1.3 mol of nickel per mol of alpha2beta2 oligomer
Nickel
-
contains 1.3 mol of Ni2+ per mol of tetramer
Nickel
-
CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
Nickel
-
the alphabeta dimer contains approximately 2 mol of nickel per mol of dimer
Nickel
-
contains 2 mol of nickel per mol of alphabeta dimer
Nickel
-
contains 2-3 mol of nickel per mol of enzyme
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 NiFe complex is required for catalyzing the exchange reaction and the acetyl-CoA synthase reaction
Nickel
-
enzyme form I contains 0.6 mol of nickel per mol of monomer; enzyme form II contains 1.4 mol of nickel per mol of monomer
Nickel
-
the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [4Fe-4S]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor, the nickel cation is proposed to be Ni2+ of the oxidized state of the C-center and in the one-electron-reduced state of the C-center, appears to strongly affect the redox behavior of the [4Fe-4S]2+/1+ component of the C-center
Nickel
-
Ni-depleted enzyme is still able to produce formate
Nickel
-
wild-type, 0.85 mol per mol of enzyme. Analysis of activation of wild-type and mutant apo-enzymes by nickel
Nickel
-
synthesis of an analogue of the C-cluster of Carboxydothermus hydrogenoformans with a planar Ni(II) site and attachment of an exo iron atom in the core unit NiFe4S5 and analysis of products
Zinc

-
the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
-
the alphabeta dimer contains approximately 1 mol of zinc per mol of dimer
Zinc
-
contains 1 mol of zinc per mol of alphabeta dimer
Zinc
-
enzyme form I contains 0.4 mol of zinc per mol of monomer; enzyme form II contains 0.8 mol of zinc per mol of monomer
additional information

-
no stimulation by MgSO4, CoCl2, NiCl2 and ZnSO4
additional information
-
the enzyme contains 30 Fe, 2 Ni, 1 Zn, and 1 Cu (per alpha 2 beta 2 enzyme)
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+
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12600
-
1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE
17200
-
L2,M2,S2, 2 * 75000 + 2 * 28400 + 2 * 17200, SDS-PAGE
17390
D5G1Y2; D5G1Y0; D5G1Y1;
small subunit, calculated from sequence of cDNA
17752
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
17800
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
18000
-
x * 92000 + x * 18000
19400
-
2 * 19400 + 2 * 79400, SDS-PAGE
21000
-
2 * 21000 + 2 * 89000, SDS-PAGE
28400
-
L2,M2,S2, 2 * 75000 + 2 * 28400 + 2 * 17200, SDS-PAGE
30200
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
30620
D5G1Y2; D5G1Y0; D5G1Y1;
medium subunit, calculated from sequence of cDNA
30694
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
34500
-
1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE
50000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
51400
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
53000
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
58000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
60000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
61800
-
1 * 61800, SDS-PAGE
62000
-
2 * 62000, enzyme, + electron transfer protein CooF and membrane bound [Ni-Fe] hydrogenase, six differentsubunits; 2 * 62000, SDS-PAGE, enzyme
63200
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
72000
-
beta subunit, SDS-PAGE
73000
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
75000
-
L2,M2,S2, 2 * 75000 + 2 * 28400 + 2 * 17200, SDS-PAGE
79400
-
2 * 19400 + 2 * 79400, SDS-PAGE
82000
-
alpha2,beta2, 2 * 82000 + 2 * 73000, enzyme previously thought to have an alpha3,beta3 structure, SDS-PAGE
85970
D5G1Y2; D5G1Y0; D5G1Y1;
large subunit, calculated from sequence of cDNA
86600
-
1 * 86600 + 2 * 34500 + 1 * 12600, SDS-PAGE
87224
-
L2,M2,S2, 2 * 87224 + 2 * 30694 + 2 * 17752, deduced from gene sequence, SDS-PAGE
88700
-
L2,M2,S2, 2 * 17800 + 2 * 30200 + 2 * 88700, dimer of heterotrimers, SDS-PAGE, crystal structure
92000
-
x * 92000 + x * 18000
94000
-
2 * 19000 + 2 * 94000, alpha2beta2, SDS-PAGE
120000
-
gel filtration, enzyme
155000
-
sedimentation equilibrium centrifugation
163700
-
calculated from amino acid sequence
205000
-
gradient gel electrophoresis
220000
-
nondenaturing PAGE
273500
-
deduced from amino acid sequence
300000
-
sedimentation equilibrium ultracentrifugation
450000
-
gel filtration, complex
1000000
-
the native enzyme (MW 250000 Da) forms aggregates with an MW of approximately 1000000, gradient gel electrophoresis
1600000
-
carbon monoxide dehydrogenase-corrinoid enzyme complex, gel filtration
3000000
-
high molecular weight form exists under conditions of high ionic strength, gel filtration
19000

-
2 * 19000 + 2 * 94000, alpha2beta2, SDS-PAGE
19000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
19700

-
2 * 19700 + 2 * 84500, alpha2beta2, SDS-PAGE; 2 * 84500 + 2 * 19700, alpha2beta2, SDS-PAGE
19700
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
70000

-
x * 70000, SDS-PAGE
70000
-
2 * 70000, SDS-PAGE
71000

-
3 * 71000, beta, + 3 * 78000, alpha, SDS-PAGE; 3 * 78000 + 3 * 71000, alpha3,beta3, SDS-PAGE
71000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
71000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
78000

-
3 * 71000, beta, + 3 * 78000, alpha, SDS-PAGE; 3 * 78000 + 3 * 71000, alpha3,beta3, SDS-PAGE
78000
-
2 * 50000 + 2 * 71000 + 2 * 78000, alpha2beta2gamma2, SDS-PAGE
84500

-
2 * 19700 + 2 * 84500, alpha2beta2, SDS-PAGE; 2 * 84500 + 2 * 19700, alpha2beta2, SDS-PAGE
84500
-
6 * 19700, alpha, + 6 * 84500, beta, + 6 * 63200, gamma, + 6 * 53000, delta, + 6 * 51400, epsilon, MW of the subunits of the carbon monoxide dehydrogenase-corrinoid enzyme complex, SDS-PAGE
89000

-
2 * 21000 + 2 * 89000, SDS-PAGE
89000
-
x * 89000 + x * 71000 + x * 60000 + x * 58000 + x * 19000, SDS-PAGE
161000

-
dialyzed enzyme, gel filtration; gel filtration
161000
-
pore limit gel electrophoresis
250000

-
gradient gel electrophoresis
250000
-
the native enzyme (MW 250000 Da) forms aggregates with an MW of approximately 1000000, gradient gel electrophoresis
additional information

-
the enzyme is part of a high molecular mass multienzyme complex that contains a corrinoid protein and carbon monoxide dehydrogenase and requires tetrahydrosarcinapterin as methyl group acceptor
additional information
-
CO dehydrogenase complex consists of a two-subunit nickel/iron-sulfur component and the two-subunit factor III-containing corrinoid/iron-sulfur (Co/Fe-S) component
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C56A
-
devoid of CO oxidation activity
K563L
-
very low CO oxidation activity
A121H/H122A
-
11% of wild type activity
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
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
C316S
-
0.3% of wild type activity
E115H/H116A
-
24% of wild type activity
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
H113A/H116A/H119A
-
no activity
H113A/H119A
-
15% of wild type activity
H116A
-
6% of wild type activity, in presence of imidazole, 3% of wild type activity
H116A/G117H
-
0.8% of wild type activity
H116C
-
46% of wild type activity
H116D
-
0.4% of wild type activity
H119A
-
27% of wild type activity
H122A
-
3% of wild type activity
H122A/A123H
-
72% of wild type activity
K587A
-
42% of wild type activity
K587A/H113A
-
0.7% 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
N284A
-
41% of wild type activity
N284A/H119A
-
36% of wild type activity
C338A
-
complete loss of activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C451A
-
complete loss of activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C451S
-
1.4% of wild-type specific activity. Unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C481A
-
unable to grow in the dark with CO as the energy source, amount of enzyme present in membrane fraction is similar to wild-type as well as accumulation of Ni2+
C531A
-
0.1% of wild-type specific activity
H265V
-
no CO oxidation activity in presence or absence of nickel, production of formate at same level as wild type
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
additional information

-
more than threefold induction of enzyme activity and increase in enzyme expression, as well as pyruvate oxidoreductase activity and expression, in a mutant lacking the membrane-bound energy-conserving hydrogenase Ehb
additional information
D5G1Y2; D5G1Y0; D5G1Y1;
the mutant YK002 does not produce the large subunit of CO-DH and exhibits no CO-DH activity
additional information
-
the mutant YK002 does not produce the large subunit of CO-DH and exhibits no CO-DH activity
-
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Bonam, D.; Ludden, P.W.
Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum
J. Biol. Chem.
262
2980-2987
1987
Rhodospirillum rubrum
brenda
Grahame, D.A.; Stadtman, T.C.
Carbon monoxide dehydrogenase from Methanosarcina barkeri. Disaggregation, purification, and physicochemical properties of the enzyme
J. Biol. Chem.
262
3706-3712
1987
Methanosarcina barkeri
brenda
DeMoll, E.; Grahame, D.A.; Harnly, J.M.; Tsai, L.; Stadtman, T.C.
Purification and properties of carbon monoxide dehydrogenase from Methanococcus vannielii
J. Bacteriol.
169
3916-3920
1987
Methanococcus vannielii
brenda
Fuchs, G.
CO2 fixation in acetogenic bacteria: variations on a theme
FEMS Microbiol. Rev.
39
181-213
1986
Acetobacterium woodii, Clostridium pasteurianum, Moorella thermoacetica
-
brenda
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
brenda
Diekert, G.; Ritter, M.
Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum
FEBS Lett.
151
141-144
1983
Moorella thermoacetica
-
brenda
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
brenda
Bott, M.H.; Eikmanns, B.; Thauer, R.K.
Defective formation and/or utilization of carbon monoxide in H2/CO2 fermenting methanogens dependent on acetate as carbon source
Arch. Microbiol.
143
266-269
1985
Autotrophic methanogenic bacterium, no activity in Methanobrevibacter ruminantium, no activity in Methanobrevibacter smithii, no activity in Methanococcus voltae, no activity in Methanospirillum hungatei
-
brenda
Daniels, L.; Fuchs, G.; Thauer, R.K.; Zeikus, J.G.
Carbon monoxide oxidation by methanogenic bacteria
J. Bacteriol.
132
118-126
1977
Methanothermobacter thermautotrophicus
brenda
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
-
brenda
Wood, H.G.; Ragsdale, S.W.; Pezacka, E.
The acetyl-CoA pathway of autotrophic growth
FEMS Microbiol. Rev.
39
345-362
1986
Acetobacterium woodii, Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Moorella thermoacetica
-
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda
Eggen, R.I.L.; van Kranenburg, R.; Vriesema, A.J.M.; Geerling, A.C.M.; Verhagen, M.F.J.M.; Hagen, W.R.; de Vos, W.M.
Carbon monoxide dehydrogenase from Methanosarcina frisia Gö1
J. Biol. Chem.
271
14256-14263
1996
Methanosarcina mazei
brenda
Spangler, N.J.; Lindahl, P.A.; Bandarian, V.; Ludden, P.W.
Spectroelectrochemical characterization of the metal centers in carbon monoxide dehydrogenase (CODH) and nickel-deficient CODH from Rhodospirillum rubrum
J. Biol. Chem.
271
7973-7977
1996
Rhodospirillum rubrum
brenda
Grahame, D.A.
Substrate and cofactor reactivity of a carbon monoxide dehydrogenase-corrinoid enzyme complex: stepwise reduction of iron-sulfur and corrinoid centers, the corrinoid Co2+/1+ redox midpoint potential, and overall synthesis of acetyl-CoA
Biochemistry
32
10786-10793
1993
Methanosarcina barkeri
brenda
Hyman, M.R.; Ensign, S.A.; Arp, D.J.; Ludden, P.W.
Carbonyl sulfide inhibition of CO dehydrogenase from Rhodospirillum rubrum
Biochemistry
28
6821-6826
1989
Rhodospirillum rubrum
brenda
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
brenda
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
brenda
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
brenda
Jablonski, P.E.; Ferry, J.G.
Reductive dechlorination of trichloroethylene by the CO-reduced CO dehydrogenase enzyme complex from Methanosarcina thermophila
FEMS Microbiol. Lett.
96
55-60
1992
Methanosarcina thermophila
brenda
Möller-Zinkhan, D.; Thauer, R.K.
Anaerobic lactate oxidation to 3 CO2 by Archaeoglobus fulgidus via the carbon monoxide dehydrogenase pathway: demonstration of the acetyl-CoA carbon-carbon cleavage reaction in cell extract
Arch. Microbiol.
153
215-218
1990
Archaeoglobus fulgidus
-
brenda
Terlesky, K.C.; Fery, J.G.
Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila
J. Biol. Chem.
263
4075-4079
1988
Methanosarcina thermophila
brenda
Jetten, M.S.M.; Stams, A.J.M.; Zehnder, A.J.B.
Purification and characterization of an oxygen-stable carbon monoxide dehydrogenase of Methanothrix soehngenii
Eur. J. Biochem.
181
437-441
1989
Methanosaeta concilii
brenda
Grahame, D.A.
Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex
J. Biol. Chem.
266
22227-22233
1991
Methanosarcina barkeri
brenda
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
brenda
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
-
brenda
Lu, W.P.; Jablonski, P.E.; Rasche, M.; Ferry, J.G.; Ragsdale, S.W.
Characterization of the metal centers of the Ni/Fe-S component of the carbon monoxide dehydrogenase enzyme complex from Methanosarcina thermophila
J. Biol. Chem.
269
9736-9742
1994
Methanosarcina thermophila
brenda
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
Oligotropha carboxidovorans
brenda
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
brenda
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
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
Lorite, M.J.; Tachil, J.; Sanjuan, J.; Meyer, O.; Bedmar, E.J.
Carbon monoxide dehydrogenase activity in Bradyrhizobium japonicum
Appl. Environ. Microbiol.
66
1871-1876
2000
Bradyrhizobium japonicum
brenda
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
brenda
Craft, J.L.; Ludden, P.W.; Brunold, T.C.
Spectroscopic Studies of Nickel-deficient Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum: Nature of the Iron-Sulfur Clusters
Biochemistry
41
1681-1688
2002
Rhodospirillum rubrum
brenda
Feng, J.; Lindahl, P.A.
Carbon monoxide dehydrogenase from Rhodospirillum rubrum: effect of redox potential on catalysis
Biochemistry
43
1552-1559
2004
Rhodospirillum rubrum
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Heo, J.; Skjeldal, L.; Staples, C.R.; Ludden, P.W.
Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate
J. Biol. Inorg. Chem.
7
810-814
2002
Rhodospirillum rubrum
brenda
Volbeda, A.; Fontecilla-Camps, J.C.
Crystallographic evidence for a CO/CO(2) tunn