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1,1,2,2-tetramethylcyclopropane + NADH + O2
?
-
-
-
-
?
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
2,3-dimethylpentane + NAD(P)H + O2
3,4-dimethylpentan-2-ol + NAD(P)+ + H2O
-
-
-
?
2-methylpropane + NAD(P)H + O2
2-methylpropan-2-ol + 2-methylpropan-1-ol + NAD(P)+ + H2O
-
-
-
?
adamantane + NAD(P)H + O2
1-adamantanol + 2-adamantanol + NAD(P)+ + H2O
-
-
-
?
ammonia + NAD(P)H + O2
hydroxylamine + NAD(P)+ + H2O
-
-
-
-
?
ammonia + NADH + H+ + O2
?
-
-
-
-
?
benzene + NAD(P)H + H+ + O2
phenol + hydroquinone + NAD(P)+ + H2O
benzene + NAD(P)H + H+ + O2
phenol + NAD(P)+ + H2O
benzene + NADH + H+ + O2
?
beta-pinene + NAD(P)H + O2
6,6-dimethylbicyclo[3.1.1]hept-2-ene-2-methanol + beta-pinene oxide + NAD(P)+ + H2O
-
-
-
?
biphenyl + NAD(P)H + H+ + O2
2-hydroxybiphenyl + 4-hydroxybiphenyl + NAD(P)+ + H2O
-
-
-
-
?
bromobenzene + NAD(P)H + O2
bromophenol + NAD(P)+ + H2O
-
sMMO
-
?
bromomethane + NAD(P)H + O2
?
bromomethane + NADH + H+ + O2
?
-
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
butylene + NAD(P)H + O2
butylene oxide + NAD(P)+ + H2O
-
sMMO
-
?
carbon monoxide + NADH + H+ + O2
?
-
-
-
-
?
chlorobenzene + NAD(P)H + O2
chlorophenol + NAD(P)+ + H2O
-
sMMO
-
?
chloromethane + NAD(P)H + O2
formaldehyde + NAD(P)+ + H2O + ?
-
-
-
?
chloromethane + NADH + H+ + O2
?
-
-
-
-
?
chloronaphthalene + NAD(P)H + O2
chloronaphthol + NAD(P)+ + H2O
-
sMMO
-
?
chloropentane + NAD(P)H + O2
chloropentanol + NAD(P)+ + H2O
-
sMMO
-
?
cis-1,3-dimethylcyclohexane + NAD(P)H + O2
3,5-dimethylcyclohexanol + 1-cis-3-dimethylcyclohexanol + NAD(P)+ + H2O + 1-trans-3-dimethylcyclohexanol
-
-
1-trans-3-dimethylcyclohexanol is produced in a low concentration
?
cis-1,4-dimethylcyclohexane + NAD(P)H + O2
1-cis-4-dimethylcyclohexanol + NAD(P)+ + H2O + trans-2,5-dimethylcyclohexanol
-
-
trans-2,5-dimethylcyclohexanol is produced in a low concentration
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
cycloheptanecarboxylate + NADH + H+ + O2
trans-4-hydroxycycloheptane-1-carboxylate + NAD+ + H2O
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
cyclohexanecarboxylate + NADH + H+ + O2
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ + H2O
cyclohexene + NAD(P)H + O2
epoxycyclohexane + 2-cyclohexen-1-ol + NAD(P)+ + H2O
-
-
-
?
cyclopentanecarboxylate + NADH + H+ + O2
trans-3-hydroxycyclopentane-1-carboxylate + NAD+ + H2O
cytochrome c + NAD(P)H + O2
reduced cytochrome c + NAD(P)+ + H2O
-
sMMO
-
-
?
dichloroethane + NADH + O2
ethanol + 2 Cl- + NAD+ + H2O
dichloromethane + NAD(P)H + O2
CO + Cl- + NAD(P)+ + H2O
-
-
-
?
dichloropropane + NADH + O2
propanol + 2 Cl- + NAD+ + H2O
-
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
dimethyl ether + NADH + H+ + O2
?
-
-
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
ethane + NADH + O2
?
-
-
-
-
?
ethane + NADH + O2
ethanol + NAD+ + H2O
-
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
ethylbenzene + NAD(P)H + H+ + O2
1-phenylethanol + 3-ethylphenol + 4-ethylphenol + NAD(P)+ + H2O
-
-
-
-
?
ethylbenzene + NAD(P)H + H+ + O2
?
molecular dynamics simulation to rationalize regioselective hydroxylation of aromatic substrates
-
-
?
fluorobenzene + NAD(P)H + O2
fluorophenol + NAD(P)+ + H2O
-
sMMO
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
formate + NAD(P)H + O2
?
-
assay with whole cells
-
-
?
furan + NAD(P)H + O2
?
-
-
-
-
?
furan + NADH + O2
? + NAD+ + H2O
-
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
heptane + NADH + O2
1-heptanol + 2-heptanol + NAD+ + H2O
-
-
-
-
?
heptanoate + NADPH + H+ + O2
? + NADP+ + H2O
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
hexanoate + NADH + H+ + O2
? + NAD+ + H2O
isobutane + NAD(P)H + O2
2-methyl-1-propanol + 2-methyl-2-propanol + NADP+ + H2O
-
-
-
?
isopentane + NAD(P)H + O2
2-methylbutan-1-ol + 3-methylbutan-1-ol + 2-methylbutan-2-ol + 3-methylbutan-2-ol + NADP+ + H2O
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
methane + NADH + H+ + O2
methanol + H2O + NAD+
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
methane + NADH + O2
methanol + NAD+ + H2O
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
methane + trans-dichloroethylene + vinyl chloride + trichloroethylene + ?
formaldehyde + ?
-
each of these compounds is completely degraded by sMMO-expressing cells when initial concentrations are either 0.01 or 0.03 mM
-
-
?
methanol + NADH + H+ + O2
? + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
methylamine + NADH + H+ + O2
hydroxymethylamine + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
methylcyanide + NADH + H+ + O2
hydroxymethylcyanide + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, and proposed mechanism of CH3CN hydroxylation by Hperoxo, overview
-
-
?
methylene cyclohexane + NAD(P)H + O2
1-cyclohexane-1-methanol + methylene cyclohexane oxide + 4-hydroxymethylene cyclohexane + NAD(P)+ + H2O
-
-
-
?
naphthalene + NAD(P)H + H+ + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
nitrobenzene + NADH + O2
nitrophenol + NAD+ + H2O
nitromethane + NADH + H+ + O2
?
-
-
-
-
?
octane + NAD(P)H + O2
1-octanol + 2-octanol + NAD(P)+ + H2O
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
phenylalanine + NAD(P)H + O2
tyrosine + NAD(P)+ + H2O
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
propylaldehyde + NADH + H+ + O2
? + H2O + NAD+
-
substrate of intermediate species, Hperoxo and Q, kinetics, overview
-
-
?
propylene + duroquinol + O2
propylene oxide + reduced duroquinol + H2O
-
-
-
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
propylene + NADH + H+ + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + H+ + O2
propylene oxide + NAD+ + H2O
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
propylene + NADH + O2
propylene oxide + NAD+ + H2O
pyridine + NAD(P)H + O2
pyridine N-oxide + NAD(P)+ + H2O
-
-
-
?
pyridine + NADH + H+ + O2
?
-
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
styrene + NADH + H+ + O2
?
-
-
-
-
?
toluene + NAD(P)H + H+ + O2
?
molecular dynamics simulation to rationalize regioselective hydroxylation of aromatic substrates
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + cresol + NAD(P)+ + H2O
-
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + p-cresol + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + H+ + O2
cresol + NAD(P)+ + H2O
-
sMMO
-
?
toluene + NADH + H+ + O2
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
trichloromethane + NAD(P)H + O2
CO2 + Cl- + NAD(P)+ + H2O
-
-
-
?
trichloromethane + NADH + H+ + O2
?
-
-
-
-
?
xylene + NAD(P)H + O2
xylenol + NAD(P)+ + H2O
-
sMMO
-
?
additional information
?
-
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
-
-
-
?
1-butene + NAD(P)H + O2
1,2-epoxybutane + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + H+ + O2
phenol + hydroquinone + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + H+ + O2
phenol + hydroquinone + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + H+ + O2
phenol + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + H+ + O2
phenol + NAD(P)+ + H2O
-
-
-
?
benzene + NADH + H+ + O2
?
-
-
-
-
?
benzene + NADH + H+ + O2
?
-
-
-
-
?
benzene + NADH + H+ + O2
?
-
-
-
-
?
benzene + NADH + H+ + O2
?
-
-
-
-
?
bromomethane + NAD(P)H + O2
?
-
-
-
-
?
bromomethane + NAD(P)H + O2
?
-
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
only 2-butanol, sMMO
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
cis-2-butene + NAD(P)H + O2
cis-2,3-epoxybutane + cis-2-buten-1-ol + 2-butanone + NAD(P)+ + H2O
-
-
-
?
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
-
-
-
-
?
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
-
-
-
-
?
CO + NAD(P)H + O2
CO2 + NAD(P)+ + H2O
-
-
-
-
?
cycloheptanecarboxylate + NADH + H+ + O2
trans-4-hydroxycycloheptane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cycloheptanecarboxylate + NADH + H+ + O2
trans-4-hydroxycycloheptane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
sMMO
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
cyclohexanecarboxylate + NADH + H+ + O2
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cyclohexanecarboxylate + NADH + H+ + O2
trans-4-hydroxycyclohexane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cyclopentanecarboxylate + NADH + H+ + O2
trans-3-hydroxycyclopentane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
cyclopentanecarboxylate + NADH + H+ + O2
trans-3-hydroxycyclopentane-1-carboxylate + NAD+ + H2O
-
-
-
-
?
dichloroethane + NADH + O2
ethanol + 2 Cl- + NAD+ + H2O
-
-
-
-
?
dichloroethane + NADH + O2
ethanol + 2 Cl- + NAD+ + H2O
-
-
-
-
?
dichloroethane + NADH + O2
ethanol + 2 Cl- + NAD+ + H2O
-
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
sMMO
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
sMMO
-
?
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
-
-
?
dimethyl ether + NAD(P)H + O2
methanol + formaldehyde + NAD(P)+ + H2O
-
no activity
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
-
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
-
-
-
-
?
ethane + NAD(P)H + O2
ethanol + NAD(P)+ + H2O
-
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
-
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
sMMO
-
?
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
-
sMMO
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
sMMO
position of hydroxylation cannot be determined exactly
?
heptanoate + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
-
?
heptanoate + NADPH + H+ + O2
? + NADP+ + H2O
-
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
-
-
-
-
?
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + H2O
-
sMMO
position of hydroxylation cannot be determined exactly
?
hexanoate + NADH + H+ + O2
? + NAD+ + H2O
-
-
-
-
?
hexanoate + NADH + H+ + O2
? + NAD+ + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + duroquinol + O2
methanol + duroquinone + H2O
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
-
-
?
methane + NAD(P)H + H+ + O2
methanol + NAD(P)+ + H2O
presentation of experimental and computational data consistent with an open-core structure for the key intermediate in methane oxidation
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
consists of three subunits, the hydroxylase (MMOH), at which the oxidation of methane takes place, the reductase (MMOR) and a small regulating unit MMOB
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NAD(P)H + O2
methanol + NAD(P)+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + H+ + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
via diiron(IV) reaction intermediate Q, the decay rate of intermediate Q is substantially accelerated in the presence of fluuoromethane and difluoromethane
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
modeling intermolecular electron transfer in the sMMO system, interconversion of rapid and slow electron-transfer pathways, overview
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
methane is oxidized to methanol with 100% efficiency with no over-oxidation, methanol is then further oxidized by other enzymes in two electron steps to CO2
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
for the MMOH alone the rate of turnover is increased 150fold and rate constant for O2 binding is increased 1000fold in the binary complex compared to the complete enzyme
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
-
-
-
-
?
methane + NADH + O2
methanol + NAD+ + H2O
methylotrophic bacterium
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + H2O
-
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
sMMO
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
oxidized by sMMO
-
-
?
naphthalene + NAD(P)H + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
nitrobenzene + NADH + O2
nitrophenol + NAD+ + H2O
-
-
-
-
?
nitrobenzene + NADH + O2
nitrophenol + NAD+ + H2O
-
an electron is removed from nitrobenzene by Q in the first step of the reaction and then the bound hydroxyl radical formed in this process rebounds to form nitrophenol
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
sMMO
position of hydroxylation cannot be determined exactly
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
only 2-propanol, sMMO
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
only 2-propanol, sMMO
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
?
propene + NAD(P)H + O2
1,2-epoxypropane + NAD(P)+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
-
-
-
-
?
propene + NADH + H+ + O2
epoxypropane + NAD+ + H2O
-
-
-
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
propylene + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + O2
propylene epoxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
-
-
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
-
the peroxodiiron(III) intermediate that precedes Q formation in the catalytic cycle has been demonstrated to react with propylene
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
-
the peroxodiiron(III) intermediate that precedes Q formation in the catalytic cycle has been demonstrated to react with propylene
-
-
?
propylene + NADH + O2
propylene oxide + NAD+ + H2O
-
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
?
styrene + NAD(P)H + O2
styrene epoxide + NAD(P)+ + H2O
-
-
-
-
?
toluene + NADH + H+ + O2
?
-
-
-
-
?
toluene + NADH + H+ + O2
?
-
-
-
-
?
toluene + NADH + H+ + O2
?
-
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
trans-2-butene + NAD(P)H + O2
trans-2,3-epoxybutane + trans-2-buten-1-ol + NAD(P)+ + H2O
-
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
-
very non-specific oxygenase
-
-
?
additional information
?
-
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
-
-
?
additional information
?
-
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
-
?
additional information
?
-
-
a number of substituted methanes, e.g. CH3X (X) H, CH3, OH, CN, NO2, or F, react with MMOH, quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
-
-
?
additional information
?
-
-
fluoroform is no substrate
-
-
?
additional information
?
-
-
the enzyme catalyzes the selective oxidation of methane to methanol, but the enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane
-
-
?
additional information
?
-
-
the enzyme catalyzes the selective oxidation of methane to methanol, but is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane. Reactions of the two intermediate species, of Hperoxo and Q, two oxidants that are generated sequentially during the reaction of reduced protein with O, with a panel of substrates of varying C-H bond strength, double-mixing stoppedflow spectroscopy, overview. Three classes of substrates exist according to the rate-determining step in the reaction
-
-
?
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
?
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
?
additional information
?
-
multicomponent monooxygenase. The ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism
-
-
?
additional information
?
-
-
multicomponent monooxygenase. The ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism
-
-
?
additional information
?
-
the regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state
-
-
?
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
?
additional information
?
-
-
fluoroform is no substrate
-
-
?
additional information
?
-
-
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview
-
-
?
additional information
?
-
-
a number of substituted methanes, e.g. CH3X (X) H, CH3, OH, CN, NO2, or F, react with MMOH, quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
-
-
?
additional information
?
-
-
very non-specific oxygenase
-
-
?
additional information
?
-
-
broad specificity
-
-
?
additional information
?
-
the regulatory component (MMOB) of soluble methane monooxygenase (sMMO) has a unique N-terminal tail not found in regulatory proteins of other bacterial multicomponent monooxygenases. This N-terminal tail is indispensable for proper function, yet its solution structure and role in catalysis remain elusive. The oxidation state of the hydroxylase component, MMOH, modulates the conformation of the N-terminal tail in the MMOH-2MMOB complex, which in turn facilitates catalysis. The N-terminal tail switches from a relaxed, flexible conformational state to an ordered state upon MMOH reduction from the diiron(III) to the diiron(II) state
-
-
?
additional information
?
-
multicomponent monooxygenase. The ferredoxin domain of the reductase binds to the canyon region of the hydroxylase, previously determined to be the regulatory protein binding site as well. The latter thus inhibits reductase binding to the hydroxylase and, consequently, intermolecular electron transfer from the reductase to the hydroxylase diiron active site. The binding competition between the regulatory protein and the reductase may serve as a control mechanism for regulating electron transfer, and other BMM enzymes are likely to adopt the same mechanism
-
-
?
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
?
additional information
?
-
-
sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity
-
-
?
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
?
additional information
?
-
-
sMMO expressed at low copper concentration shows low substrate specificity, while pMMO expressed at high copper concentration shows high substrate specificity
-
-
?
additional information
?
-
-
Methyloferula stellata AR4 is an aerobic acidophilic methanotroph, which, in contrast to most known methanotrophs but similar to Methylocella spp., possesses only a soluble methane monooxygenase
-
-
?
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
?
additional information
?
-
-
the sMMO enzyme has broad substrate specificity compared to pMMO
-
-
?
additional information
?
-
-
the soluble methane monooxygenase receives electrons from NADH via its reductase MmoC for oxidation of methane. The NADH-dependent reductase MmoC produces only trace amounts of superoxide, but mainly hydrogen peroxide during uncoupled turnover reactions
-
-
-
additional information
?
-
-
the soluble methane monooxygenase receives electrons from NADH via its reductase MmoC for oxidation of methane. The NADH-dependent reductase MmoC produces only trace amounts of superoxide, but mainly hydrogen peroxide during uncoupled turnover reactions
-
-
-
additional information
?
-
-
pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
-
-
?
additional information
?
-
-
access and regulation in the methane monooxygenase system via interaction of reductase protein MMOB and hydroxylase protein MMOH, regulatory effects of MMOB, overview
-
-
?
additional information
?
-
-
enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds
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additional information
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sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane
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additional information
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enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds
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additional information
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sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane
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additional information
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enzyme sMMO shows oxidation ability of various substrates, including alkanes, alkenes, aromatics, heterocyclics, and chlorinated compounds
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additional information
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sMMO is known to oxidize a variety of hydrocarbons, including alkanes ranging from methane to octane. The presence of 1,6-hexanediol near the di-iron center can be explained by the opening of the cavity, mediated by the side-chain rearrangement of Leu110 and Phe188, both of which function together as a gate for substrate and product passage to the active site. While MMOB is known to connect cavities for substrate access, the MMOD-mediated cavity opening appears to be a consequence of MMOHbeta-NT dissociation and subsequent structural relaxation of MMOHalpha. Both substrate ingress and product egress may take place through the substrate access cavity and not through the pore located near the active site, at least for hydrocarbon chain substrates such as hexane
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additional information
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oxidation of norborneols
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oxidation of deuterated compounds
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effects of spin-traps on MMO activity, overview
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inactive toward anthracene and phenanthrene
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pMMO has broader substrate specificity but lower activity with smaller hydrocarbons like methane, ethane, and propene compared to pMMO
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additional information
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naphthalene assay for sMMO activity
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additional information
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a colorimetric assay is adopted for the sMMO activity detection of biofilm
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malfunction
mutations in the core region of MMOB and in the N- and C-termini cause dramatic changes in the rate constants for steps in the sMMOH reaction cycle
evolution
methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. Enzyme sMMO belongs to the larger bacterial multicomponent monooxygenase (BMM) family. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available
evolution
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enzyme sMMO belongs to the BMM superfamily
evolution
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enzyme sMMO belongs to the BMM superfamily
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evolution
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methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. Enzyme sMMO belongs to the larger bacterial multicomponent monooxygenase (BMM) family. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available
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evolution
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methanotrophs produce two genetically unrelated MMOs: soluble MMO (sMMO) expressed by a subset of methanotrophs and membrane-bound, particulate MMO (pMMO) expressed by nearly all methanotrophs. Enzyme sMMO belongs to the larger bacterial multicomponent monooxygenase (BMM) family. In organisms that have genes for both sMMO and pMMO, expression levels are coupled to intracellular copper levels in a mechanism known as the copper switch, wherein sMMO is produced at low copper concentrations while pMMO expression is mildly upregulated and sMMO expression is downregulated when copper is available
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evolution
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enzyme sMMO belongs to the BMM superfamily
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metabolism
ammonia-supplied Methylosinus trichosporium OB3b containing soluble methane monooxygenase (sMMO) grow at the fastest rate, while the highest poly-beta-hydroxybutyrate content is obtained by transferring nitrate-supplied bacteria with the expression of particulate methane monooxygenase (pMMO) to nitrogen-free mineral salts (NFMS) + 0.005 mmol/l Cu medium
metabolism
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
metabolism
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
metabolism
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Methyloceanibacter methanicus {R-67174} is capable of oxidizing methane as sole source of carbon and energy using solely a soluble methane monooxygenase
metabolism
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Methyloferula stellata AR4 is an aerobic acidophilic methanotroph, which, in contrast to most known methanotrophs but similar to Methylocella spp., possesses only a soluble methane monooxygenase
metabolism
the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO, EC 1.14.18.3, and soluble MMO, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview
metabolism
the high number of up-regulated genes in cells producing soluble methane monooxygenase shows that Methylococcus capsulatus is highly adapted to copper-limited growth
metabolism
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enzyme is a self-sufficient cytochrome P450
metabolism
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enzyme is a self-sufficient cytochrome P450
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metabolism
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the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO, EC 1.14.18.3, and soluble MMO, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview
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metabolism
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the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, analysis of the mechanism of the copper switch. Transcriptomic profiling of particulate MMO, EC 1.14.18.3, and soluble MMO, using Methylococcus capsulatus DNA microarrays. 137 ORFs are found to be differentially expressed between cells producing sMMO and pMMO, while only minor differences in gene expression are observed between the pMMO-producing cultures. Of these, 87 genes are upregulated during sMMO-producing cells, i.e. during copper-limited growth. Major changes takes place in the respiratory chain between pMMO-and sMMO-producing cells, and quinone are predominantly used as the electron donors for methane oxidation by pMMO. Proposed pathway of methane oxidation in Methylococcus capsulatus cells producing either sMMO or pMMO, overview
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metabolism
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methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
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metabolism
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the high number of up-regulated genes in cells producing soluble methane monooxygenase shows that Methylococcus capsulatus is highly adapted to copper-limited growth
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metabolism
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Methyloceanibacter methanicus {R-67174} is capable of oxidizing methane as sole source of carbon and energy using solely a soluble methane monooxygenase
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physiological function
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pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain
physiological function
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soluble methane monooxygenase is a bacterial enzyme that converts methane to methanol at a carboxylate-bridged diiron center with exquisite control. The enzyme is also capable of hydroxylating and epoxidizing a broad range of hydrocarbon substrates in addition to methane
physiological function
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MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol
physiological function
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the enzyme is strongly regulated by the availability of copper. Methanobactin produced by Methylosinus trichosporium OB3b plays a key role in controlling expression of MMO genes in this strain
physiological function
full activity of soluble methane monooxygenase (sMMO) depends upon the formation of a 1:1 complex of the regulatory protein MMOB with each alpha subunit of the (alphabetagamma)2 hydroxylase, sMMOH
physiological function
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in the enzyme complex of sMMO, Two molar equivalents of MMOB are necessary to achieve catalytic activities and oxidized a broad range of substrates including alkanes, alkenes, halogens, and aromatics. Optimal activities are observed at pH 7.5 for most substrates possibly because of the electron transfer environment in MMOR. The presence of iron at the diiron active site is required for the catalytic activity of the sMMO. Secretion of siderophores could be a defense mechanism of Methylosinus sporium strain 5 in growth condition of high bacterial concentrations and limited iron concentration. A possible explanation is that Methylosinus sporium strain 5 responds more sensitively than other type II methanotrophs because this methanotroph generates a brown-black pigment in response to a high cell:iron ratio. MMOR is an essential component for the catalytic cycle owing to its electron transfer abilities, which are accomplished by FAD-containing and [2Fe-2S] cluster ferredoxin domains to reduce diiron active sites in MMOH. NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands
physiological function
soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme capable of catalyzing the conversion of methane to methanol at ambient temperature and pressure. The enzyme consists of three protein components: a 245 kDa (alphabetagamma)2 hydroxylase (sMMOH), a 38 kDa flavin adenine dinucleotide (FAD) and 2Fe-2S cluster-containing reductase (MMOR), and a 15 kDa cofactorless regulatory component (MMOB). The sMMOH active site contains a dinuclear iron cluster, which serves to activate molecular oxygen for insertion into the C-H bond of methane. The resting state of sMMOH contains a diferric cluster (Fe3+Fe3+, sMMOHox) in which the irons are bridged by two solvent (OH- or H2O) molecules in addition to the carboxylate of Glu144. sMMOHox can form a complex with MMOR and receive two electrons to form the diferrous cluster (Fe2+Fe2+, sMMOHred) in which Glu243 shifts to bridge the irons via one carboxylate oxygen, one bridging solvent is lost, and the bond to the second solvent is weakened. In this new configuration, the diiron cluster can bind O2 between the irons upon dissociation of the weakly bound solvent. But O2 binding is observed to be very slow in the absence of the regulatory component MMOB. Binding of MMOB effects a 1000fold increase in the rate constant for the O2 binding to the diiron cluster to form the first spectroscopically distinct intermediate of the reaction cycle, termed P*. One cause of the decreased rate of O2 binding in the sMMOH active site in the absence of MMOB is the near closure of the molecular tunnel that mediates the transit of O2 from the solvent. This bottleneck is relieved by conformational changes in both MMOB and sMMOHred when the sMMOHred:MMOB complex forms. A second cause of the low reactivity of O2 with sMMOHred is the position of the Glu209 ligand to the diiron cluster, which blocks the approach to the open iron coordination site. An angle change of this residue in the sMMOHred:MMOB complex exposes the site for O2 binding. The formation of intermediate P* is followed by a spontaneous formation of a peroxo-intermediate P, and finally, O-O bond cleavage to yield the reactive dinuclear Fe4+ intermediate Q. Q can react directly with methane to form methanol with the incorporation of one atom of oxygen sourced from O2. Intermediate Q is generated and stabilized by precisely coordinated sMMO protein component interactions. Regulation of electron transfer in the sMMO system, mechanism, modeling, detailed overview. MMOR causes both the N-terminal tail and the core region of MMOB to dissociate from sMMOH
physiological function
soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme that catalyzes the conversion of methane to methanol at ambient temperature using a nonheme, oxygen-bridged dinuclear iron cluster in the active site. Structural changes in the hydroxylase component (sMMOH) containing the diiron cluster caused by complex formation with a regulatory component (MMOB) and by iron reduction are important for the regulation of O2 activation and substrate hydroxylation. The diiron cluster and the active site environment are reorganized by the regulatory protein component in order to enhance the steps of oxygen activation and methane oxidation. Although chemically reduced sMMOH can carry out the oxygenation chemistry alone, the reaction only proceeds at a physiologically relevant rate when sMMOH is complexed with MMOB. Many regulatory functions of MMOB have been discovered but its most important effects are to decrease the redox potential of the diiron cluster by 132 mV, accelerate O2 binding by 1000fold, increase the turnover number 150fold, and tune sMMOH to selectively bind and oxygenate methane over other more easily oxidized hydrocarbons
physiological function
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soluble methane monooxygenase in methanotrophs converts methane to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay of its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor for MMOH by competing with MMOB for MMOH association as well as by disrupting the active geometric form of the di-iron center. The expression level of MMOD is relatively low and it binds tightly with MMOH near the di-iron center. ApoMMOH (iron removed) in the presence of MMOD or MMOB demonstrates that both MMOD and MMOB block iron loading toward apoMMOH instead of promoting it. Both iron atoms show full occupancy at the di-iron center during structure refinement, indicating that there is no loss of iron upon MMOD association. One potential function is that MMOD acts as a protein chaperone to assist the protein folding of MMOH by protecting MMOH until MMOHbeta-NT latches on as the final step of the protein folding process, potential function of MMOD as a protein chaperone
physiological function
the metalloenzyme soluble methane monooxygenase (sMMO) consists of hydroxylase (sMMOH), regulatory (MMOB), and reductase components. When sMMOH forms a complex with MMOB, the rate constants are greatly increased for the sequential access of O2, protons, and CH4 to an oxygen-bridged diferrous metal cluster located in the buried active site
physiological function
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in the enzyme complex of sMMO, Two molar equivalents of MMOB are necessary to achieve catalytic activities and oxidized a broad range of substrates including alkanes, alkenes, halogens, and aromatics. Optimal activities are observed at pH 7.5 for most substrates possibly because of the electron transfer environment in MMOR. The presence of iron at the diiron active site is required for the catalytic activity of the sMMO. Secretion of siderophores could be a defense mechanism of Methylosinus sporium strain 5 in growth condition of high bacterial concentrations and limited iron concentration. A possible explanation is that Methylosinus sporium strain 5 responds more sensitively than other type II methanotrophs because this methanotroph generates a brown-black pigment in response to a high cell:iron ratio. MMOR is an essential component for the catalytic cycle owing to its electron transfer abilities, which are accomplished by FAD-containing and [2Fe-2S] cluster ferredoxin domains to reduce diiron active sites in MMOH. NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands
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physiological function
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soluble methane monooxygenase in methanotrophs converts methane to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay of its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor for MMOH by competing with MMOB for MMOH association as well as by disrupting the active geometric form of the di-iron center. The expression level of MMOD is relatively low and it binds tightly with MMOH near the di-iron center. ApoMMOH (iron removed) in the presence of MMOD or MMOB demonstrates that both MMOD and MMOB block iron loading toward apoMMOH instead of promoting it. Both iron atoms show full occupancy at the di-iron center during structure refinement, indicating that there is no loss of iron upon MMOD association. One potential function is that MMOD acts as a protein chaperone to assist the protein folding of MMOH by protecting MMOH until MMOHbeta-NT latches on as the final step of the protein folding process, potential function of MMOD as a protein chaperone
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physiological function
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MMO is an enzyme complex that can oxidize the C-H bonds in methane and other alkanes. As one of the oxidoreductase group,MMOplays a critical role in the first step of methanotrophs metabolism where methane is transformed into methanol
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physiological function
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in the enzyme complex of sMMO, Two molar equivalents of MMOB are necessary to achieve catalytic activities and oxidized a broad range of substrates including alkanes, alkenes, halogens, and aromatics. Optimal activities are observed at pH 7.5 for most substrates possibly because of the electron transfer environment in MMOR. The presence of iron at the diiron active site is required for the catalytic activity of the sMMO. Secretion of siderophores could be a defense mechanism of Methylosinus sporium strain 5 in growth condition of high bacterial concentrations and limited iron concentration. A possible explanation is that Methylosinus sporium strain 5 responds more sensitively than other type II methanotrophs because this methanotroph generates a brown-black pigment in response to a high cell:iron ratio. MMOR is an essential component for the catalytic cycle owing to its electron transfer abilities, which are accomplished by FAD-containing and [2Fe-2S] cluster ferredoxin domains to reduce diiron active sites in MMOH. NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands
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physiological function
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soluble methane monooxygenase in methanotrophs converts methane to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay of its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor for MMOH by competing with MMOB for MMOH association as well as by disrupting the active geometric form of the di-iron center. The expression level of MMOD is relatively low and it binds tightly with MMOH near the di-iron center. ApoMMOH (iron removed) in the presence of MMOD or MMOB demonstrates that both MMOD and MMOB block iron loading toward apoMMOH instead of promoting it. Both iron atoms show full occupancy at the di-iron center during structure refinement, indicating that there is no loss of iron upon MMOD association. One potential function is that MMOD acts as a protein chaperone to assist the protein folding of MMOH by protecting MMOH until MMOHbeta-NT latches on as the final step of the protein folding process, potential function of MMOD as a protein chaperone
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physiological function
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pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain
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additional information
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analysis of structural and functional differences of sMMO and pMMO, EC 1.14.18.3, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview. Structural architecture of sMMO. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), structure-function relationships, detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site, sMMOH docking simulations. MMOB acts as a controller of the methane-to-methanol conversion reaction
additional information
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enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
additional information
enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
additional information
enzyme sMMO structural reorganization through subunits MMOH and MMOB including the dinuclear iron cluster, detailed overview
additional information
exogenous ligands bound to the diiron cluster of the sMMOH:MMOB complex induce conformational changes, structural analysis, overview. Bottlenecks between cavities are regulated by flexible residues. Bottleneck regulated by residues V105, F109, V285, and L289 is located between cavities 3 and 2. Cavity 2 is separated from the active site cavity 1 by another bottleneck controlled by residues L110, F188, L216, F282 and F286. Cavities 3 and 2 are connected in all of the Mt sMMOH and sMMOH:MMOB crystal structures. The MMOB binding-induced reorganization of the bottleneck residues L216 and L110 in sMMOH serves to isolate cavity 1 from cavity 2 in the complex. The pore is located between helices E and F and has been proposed to be involved in regulating the access of substrates and release of products (CH3OH) to and from the active site, respectively. The strictly conserved amino acids T213, N214, and E240 are considered the pore gating residues that regulate these processes. The pore is a uniquely polar region on the sMMOH surface as it is flanked by hydrophobic amino acids A210, V218, L237, L244, and M247 on helices E and F. The side chain of T213 lines the active site cavity and the hydroxyl moiety points towards the diiron cluster. Chemical reduction of the diiron cluster causes the middle of helix E to twist, resulting in T213 and N214 to shift 2.2 A and 3.2 A, respectively. The rotameric conformations of the hydrophobic residues V218, L244, and M247 are altered as well, helping to create a chemical environment that does not favor stable binding of water molecules to the region around the pore. MMOB binding to sMMOH causes structural rearrangement of the pore residues as well. The side chain of E240 is no longer solvent exposed, and instead, traverses the width of the Pore. This new conformation blocks the access of substrates through the Pore into the active site cavity. The side chain of T213 is shifted 2.2 A compared to its position in Mt sMMOHox and rotated about 180° compared to its position in Mt sMMOHred. This new conformation positions the side chain hydroxyl moiety of T213 to face away from the diiron cluster and form a hydrogen bond with E240. MMOB covers the pore while in complex with sMMOH, further limiting access to the active site by this route
additional information
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exogenous ligands bound to the diiron cluster of the sMMOH:MMOB complex induce conformational changes, structural analysis, overview. Bottlenecks between cavities are regulated by flexible residues. Bottleneck regulated by residues V105, F109, V285, and L289 is located between cavities 3 and 2. Cavity 2 is separated from the active site cavity 1 by another bottleneck controlled by residues L110, F188, L216, F282 and F286. Cavities 3 and 2 are connected in all of the Mt sMMOH and sMMOH:MMOB crystal structures. The MMOB binding-induced reorganization of the bottleneck residues L216 and L110 in sMMOH serves to isolate cavity 1 from cavity 2 in the complex. The pore is located between helices E and F and has been proposed to be involved in regulating the access of substrates and release of products (CH3OH) to and from the active site, respectively. The strictly conserved amino acids T213, N214, and E240 are considered the pore gating residues that regulate these processes. The pore is a uniquely polar region on the sMMOH surface as it is flanked by hydrophobic amino acids A210, V218, L237, L244, and M247 on helices E and F. The side chain of T213 lines the active site cavity and the hydroxyl moiety points towards the diiron cluster. Chemical reduction of the diiron cluster causes the middle of helix E to twist, resulting in T213 and N214 to shift 2.2 A and 3.2 A, respectively. The rotameric conformations of the hydrophobic residues V218, L244, and M247 are altered as well, helping to create a chemical environment that does not favor stable binding of water molecules to the region around the pore. MMOB binding to sMMOH causes structural rearrangement of the pore residues as well. The side chain of E240 is no longer solvent exposed, and instead, traverses the width of the Pore. This new conformation blocks the access of substrates through the Pore into the active site cavity. The side chain of T213 is shifted 2.2 A compared to its position in Mt sMMOHox and rotated about 180° compared to its position in Mt sMMOHred. This new conformation positions the side chain hydroxyl moiety of T213 to face away from the diiron cluster and form a hydrogen bond with E240. MMOB covers the pore while in complex with sMMOH, further limiting access to the active site by this route
additional information
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interaction analysis of sMMO subunits and structure-function analysis, detailed overview. Alterations of hydrogen bonding or solvent accessibility occur due to the conformational changes of isoalloxazine in FAD
additional information
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MmoC homology modeling using structure PDB ID 1KRH.1 and the crystal structure of the monomeric MMOH-MmoB complex from Methylococcus capsulatus (PDB ID 4GAM) as a templates
additional information
significant conformational changes must be imparted within sMMOH by the binding of MMOB. Small-molecule tunnel analysis, overview
additional information
soluble methane monooxygenase component interactions monitored by 19F NMR spectroscopy. Modeling for regulation in which the dynamic equilibration of MMOR and MMOB with sMMOH allows a transient formation of key reactive complexes that irreversibly pull the reaction cycle forward. The slow kinetics of exchange of the sMMOH:MMOB complex is proposed to prevent MMOR-mediated reductive quenching of the high-valent reaction cycle intermediate Q before it can react with methane
additional information
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structure comparisons of the enzymes from Methylosinus sporium strain 5 and Methylosinus trichosporium strain OB3b. MMOH-MMOD complex modeling, overview
additional information
structure-spectroscopy correlations for intermediate Q of soluble methane monooxygenase, QM/MM calculations. Modeling of the MMOH oxidative and reductive state, Moessbauer parameters and electronic structure of MMOHox. The selection of plausible models include the following: (1) bis-mu-oxo bridged cores, (2) mu-OepsilonGlu243 bridged diamond cores, inspired from the MMOHred structure, as suggested recently, (3) mu-oxo bridged open cores, and (4) mu-OepsilonGlu243 bridged open cores. Closed- and open-core conformations for the key intermediate in sMMO. Optimized cores of eight MOHQ models are analyzed for molecular structure and electronic structure
additional information
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interaction analysis of sMMO subunits and structure-function analysis, detailed overview. Alterations of hydrogen bonding or solvent accessibility occur due to the conformational changes of isoalloxazine in FAD
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additional information
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structure comparisons of the enzymes from Methylosinus sporium strain 5 and Methylosinus trichosporium strain OB3b. MMOH-MMOD complex modeling, overview
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additional information
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enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
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additional information
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analysis of structural and functional differences of sMMO and pMMO, EC 1.14.18.3, substrate/product/cofactor-active site interactions, docking analysis of interactions between cofactors and corresponding enzymes. Molecular simulations and modeling, overview. Structural architecture of sMMO. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), structure-function relationships, detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site, sMMOH docking simulations. MMOB acts as a controller of the methane-to-methanol conversion reaction
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additional information
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MmoC homology modeling using structure PDB ID 1KRH.1 and the crystal structure of the monomeric MMOH-MmoB complex from Methylococcus capsulatus (PDB ID 4GAM) as a templates
-
additional information
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enzyme sMMO contains a non-heme diiron active site, active site structure, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
-
additional information
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interaction analysis of sMMO subunits and structure-function analysis, detailed overview. Alterations of hydrogen bonding or solvent accessibility occur due to the conformational changes of isoalloxazine in FAD
-
additional information
-
structure comparisons of the enzymes from Methylosinus sporium strain 5 and Methylosinus trichosporium strain OB3b. MMOH-MMOD complex modeling, overview
-
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?
-
component A: 2 * 55000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
?
-
protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
?
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
?
the hydroxylase (MMOH) component is a homodimer that consists of two protomers, and each protomer has three polypeptides (alphabetagamma), 60600 (alpha/MmoX) + 40500 (beta/MmoY) + 19800 (gamma/MmoZ), two equivalent of the regulatory component (MmoB) bind to one equivalent MMOH (alpha2beta2gamma2), + reductase protein (MmoC), + 12000 (MmoD)
?
-
protein A: 2 * 54000-60630, alpha+ 2 * 42000-44720, beta + 2 * 17000-19840, gamma
-
?
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
-
?
-
the hydroxylase (MMOH) component is a homodimer that consists of two protomers, and each protomer has three polypeptides (alphabetagamma), 60600 (alpha/MmoX) + 40500 (beta/MmoY) + 19800 (gamma/MmoZ), two equivalent of the regulatory component (MmoB) bind to one equivalent MMOH (alpha2beta2gamma2), + reductase protein (MmoC), + 12000 (MmoD)
-
?
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
?
-
component A of sMMO: 2 * 57000 + 2 * 43000 + 2 * 23000, alpha2beta2gamma2, SDS-PAGE
-
?
-
x * 37900, SDS-PAGE
-
?
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
?
-
component A: 2 * 56000 alpha + 2 * 40000 beta + 2 * 20000 gamma, SDS-PAGE
-
?
-
component A: 2 * 54400 alpha, 2 * 43000 beta + 2 * 22700 gamma, sedimentation velocity, SDS-PAGE, amino acid analysis
dimer
-
component D of sMMO: 2 * 12000, SDS-PAGE
dimer
-
component D of sMMO: 2 * 12000, SDS-PAGE
-
dimer
-
component B: 2 * 15100, SDS-PAGE
heterotrimer
-
heterotrimer
-
1 * 42000 + 1 * 24000 + 1 * 22000, SDS-PAGE
hexamer
-
(alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE
hexamer
-
(alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE
-
hexamer
-
(alphabetagamma)2, 1 * 59900, alpha-subunit, + 1 * 45200, beta-subunit, 1 * 19300, gamma-subunit, SDS-PAGE
-
hexamer
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
hexamer
-
2 * 58000, alpha-subunit, + 2 * 36000, beta-subunit, + 2 * 23000, gamma-subunit, (alphabetagamma)2, SDS-PAGE
-
trimer
1 * 245000, alpha-subunitMMOH, + 1 * 37000, beta-subunit MMOR, + 1 * 15000, gamma-subunit MMOB
trimer
soluble methane monooxygenase (sMMO) is a multicomponent metalloenzyme, all three sMMO protein components are: hydroxylase (MMOH), reductase (MMOR), and regulatory protein (MMOB), (alphabetagamma)2, 1 * 245000, hydroxylase (sMMOH), + 1 * 38000, flavin adenine dinucleotide (FAD) and 2Fe-2S cluster-containing reductase (MMOR) + 1 * 1000 cofactorless regulatory component (MMOB)
additional information
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see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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see under molecular weight for the size of the protein components
additional information
-
see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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structure, review
additional information
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component A is a hydroxylase
additional information
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component A is a hydroxylase
additional information
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component A is a hydroxylase
additional information
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component A is a hydroxylase
additional information
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component A is a hydroxylase
additional information
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sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D
additional information
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enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview
additional information
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enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
additional information
enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
additional information
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structural architecture of sMMO, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site
additional information
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enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
-
additional information
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structural architecture of sMMO, overview. Enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview. MMOR consists of a NAD binding domain, an FAD-binding domain and a ferredoxin and plays a key role in the delivery of electrons within sMMO enzyme systems. The Fe2S2 domain appears to be the MMOH (methane monooxygenase hydroxylase) binding site
-
additional information
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enzyme structure, the enzyme consists of a hydroxylase protein MMOH and a regulatory reductase protein MMOR, comparison of MMOH-MMOR-ferrdoxin and MMOH-MMOR, binding interactions, overview
-
additional information
-
see under molecular weight for the size of the protein components
-
additional information
-
enzyme system consists of 3 protein components A, B, C
-
additional information
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component A is a hydroxylase
-
additional information
-
structure, review
-
additional information
-
sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D
-
additional information
-
enzyme sMMO requires three protein components for maximal catalytic activity: the hydroxylase (MMOH), the reductase (MMOR), and the regulatory protein (MMOB), detailed overview
-
additional information
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sMMO is a multicomponent enzyme consisting of a hydroxylase, a protein B and a reductase
additional information
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three-dimensional structure, the enzyme consists as three protein component system, the regulatory protein MMOB, containing Fe2S2 cluster and a FAD cofactor, binds to the active site-containing hydroxylase protein creating a pore sized for methane into the active site, the third component is termed B, the complex appears to cause quantum tunneling to dominate in CH bond cleavage reaction for methane, selectively increasing the rate for this substrate, overview
additional information
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see under molecular weight for the size of the protein components
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)
additional information
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the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)
-
additional information
-
see under molecular weight for the size of the protein components
-
additional information
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enzyme system consists of 3 protein components A, B, C
-
additional information
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the enzyme complex of sMMO is formed by different components, including hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR)
-
additional information
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complex formation of protein components
additional information
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see under molecular weight for the size of the protein components
additional information
-
see under molecular weight for the size of the protein components
additional information
-
see under molecular weight for the size of the protein components
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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enzyme system consists of 3 protein components A, B, C
additional information
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3 components: 1 soluble CO-binding cytochrome c, 1 copper-containing protein, and 1 small protein, SDS-PAGE
additional information
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component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
-
component A is a hydroxylase
additional information
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interaction of the soluble methane monooxygenase regulatory component, MMOB, and the active site-bearing hydroxylase component, MMOH, spin labeling with 4-maleimido-2,2,6,6-tetramethyl-1-piperidinyloxy, high affinity of labeled MMOB for the oxidized MMOH decreases substantially with increasing pH and increasing ionic strength but is nearly unaffected by addition of nonionic detergents, the MMOB-MMOH complex is stabilized by electrostatic interactions, overview
additional information
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the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
additional information
the sMMO enzyme consists of three protein components: a 245 kDa (alphabetagamma)2 hydroxylase (MMOH), a 37 kDa FAD and Fe2S2 cluster-containing reductase (MMOR), and a 15 kDa regulatory protein (MMOB). The active site is buried deep within sMMOH and contains an oxygen-bridged dinuclear FeIII cluster in which the irons are bridged by two hydroxo moieties and a carboxylate from Glu144. After reduction, the diiron cluster functions to activate O2 and insert an oxygen atom into a highly stable (105 kcal/mol bond dissociation energy) C-H bond of methane. Although chemically reduced sMMOH can carry out the oxygenation chemistry alone, the reaction only proceeds at a physiologically relevant rate when sMMOH is complexed with MMOB. Reduction of the diiron cluster causes a shift in the position of Glu243, a monodentate ligand to Fe2 in the diferric cluster. In the shifted position, Glu243 bridges Fe1 and Fe2 via one of its carboxylate oxygens, thereby directly displacing one of the bridging solvents. The second bridging solvent bond is weakened, which presumably allows facile displacement by O2 to begin the oxygen activation process
additional information
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the enzyme mainly exists of alpha-helical regions, circular dichroism measurement
-
additional information
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protein comprises a [2Fe-2S] ferredoxin domain, NAD(P)H-dependent FAD-containing reductase domain, FCD domain, and cytochrome P450 domain, in that order from the N terminus
additional information
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protein comprises a [2Fe-2S] ferredoxin domain, NAD(P)H-dependent FAD-containing reductase domain, FCD domain, and cytochrome P450 domain, in that order from the N terminus
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A115C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
A62C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview, the mutant MMOH-MMOB complex is perturbed by salts but not nonionic detergents
D71C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
D87C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
G119C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
H33A
site-directed mutagenesis, an N-terminal region variant, structure analysis
H5A
site-directed mutagenesis, an N-terminal region variant, structure analysis
K44C
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site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
L110C
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110G
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110R
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl, and ethylbenzene as a substrate compared to the wild type enzyme
L110Y
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mutant shows inverted or shifted regioselectivity with naphthalene, biphenyl and ethylbenzene as a substrate compared to the wild type enzyme
N107G/S109A/S110A/T111A
site-directed mutagenesis, mutations in the core region, termed the Quad variant, structure analysis
N107G/S110A
site-directed mutagenesis, a binary derivative of the Quad variant, termed DBL1. The DBL1 mutation in MMOB leads to a loss of the S110 hydrogen bond with N214 of the sMMOH alpha-subunit, structure analysis
R133C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
S109A/T111A
site-directed mutagenesis, a binary derivative of the Quad variant, termed DBL2, structure analysis
S109C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
T111C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
V39C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
V39F
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V39R
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V41E
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V41F
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V41R
site-directed mutagenesis in the MMOB component, the mutant component variant nearly halts the reaction of the reconstituted sMMO system
V68C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
W77F
site-directed mutagenesis in the MMOB component
Y102C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
G10A/G13Q/G16A
-
reduced activity
G10A/G13Q/G16A
-
His-tagged protein B of sMMO, triple mutant is resistant to degradation in contrast to the wild-type, N-terminus is responsible for unusual mobility in size exclusion chromatography and proteolytic sensitivity of protein B
G13Q
-
reduced activity
G13Q
-
enhanced temperature stability compared to wild-type, site-directed mutagenesis
G13Q
-
sMMO, alteration of a cleavage site in component protein B
G10A/G13Q/G16A
-
reduced activity
-
G10A/G13Q/G16A
-
His-tagged protein B of sMMO, triple mutant is resistant to degradation in contrast to the wild-type, N-terminus is responsible for unusual mobility in size exclusion chromatography and proteolytic sensitivity of protein B
-
G13Q
-
reduced activity
-
G13Q
-
sMMO, alteration of a cleavage site in component protein B
-
K15C
-
site-directed mutagenesis of enzyme component MMOH, mobility and accessibility parameters for the spin-labeled MMOB mutants alone and in complex with MMOH in comparison to the wild-type enzyme, overview
K15C
site-directed mutagenesis in the MMOB component
T111Y
-
mutant enzyme with increased rate constant for the reaction of large substrates such as ethane, furan, and nitrobenzene with the reactive MMOH (regulatory componant of the enzyme) intermediate Q while decreasing the rate constant for the reaction with methane. The regiospecificity for nitrobenzene oxidation is altered and 10fold more T111Y than wild-type MMOB is required to maximize the rate of turnover
T111Y
-
the T111Y variant of MMOB causes only a small increase in reactivity
additional information
-
native parallel occurence of full length and 2 N-terminal truncated forms of regulatory component protein B of sMMO, truncated forms are inactive
additional information
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mutagenesis of MMOB potentially broadening the substrate range of the enzyme
additional information
-
substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5
additional information
-
substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5
-
additional information
-
substitution of MMOB or MMOR from another type II methanotroph, Methylocystis species M, retains specific enzyme activities, demonstrating the successful cross-reactivity of Methylosinus sporium strain 5
-
additional information
-
construction of deletion mutants of subunit MMOB missing 5, 8, and 13 C-terminal residues, the mutations cause progressive decreases in the maximum steady-state turnover number, as well as lower apparent rate constants for formation of the key reaction cycle intermediate compound Q, the deletions result in substantial uncoupling at or before the P intermediate due to competition between slow H2O2 release from one of the intermediates and the reaction that carries this intermediate on to the next step in the cycle, which is slowed by the mutation
additional information
construction of N- and C-terminal truncation variants. The dramatic effects of specific mutations on specific steps of the reaction cycle include the (i) retarding O2-binding (MMOB DELTA2-29 and V41R), (ii) uncoupling the O2-activation reaction from hydrocarbon oxidation (MMOB DELTA126-138), (iii) relaxing the size-selective entry of hydrocarbon substrates (Quad, DBL2), (iv) disrupting the quantum-tunneling nature of the HAT reaction of Q with methane (Quad), and (v) significantly increasing or decreasing the rate constants of reaction cycle steps (H33A, DBL1, DELTA126-138, H5A, V41R, and V39R). Effect of the MMOB variants on small-molecule access tunnels, overview
additional information
establishing of a methanotrophic co-metabolic system, built in the gcSBBR seeded by soil at a ventilation opening of coal mine in the presence of Cu2+, and seeded with sMMO in Methylosinus trichosporium OB3b and particulate methane monooxygenase (pMMO) in Methylocystis parvus in a biofilm, microbial community analyses and microbial 16S rRNA sequencing, and postulated pathway of methanotrophic co-metabolic system, overview. Six kinds of methanotrophs are detected from the seeded soil, namely, Methylocystis (0.29%), Methylocystaceae_unclassified (0.16%), Methylocystaceae_uncultured (0.04%) and Methylocaldum (0.14%), Methylococcaceae_unclassified (0.10%), Methylobacteriaceae_uncultured (0.04%), totally accounting for 0.77%
additional information
kinetic analysis of MMOB mutants, overview
additional information
-
kinetic analysis of MMOB mutants, overview
additional information
the two tryptophan residues in MMOB and the single tryptophan residue in MMOR are converted to 5-fluorotryptophan (5FW) by expression in defined media containing 5-fluoroindole. In addition, the mechanistically significant N-terminal region of MMOB is 19F-labeled by reaction of the K15C variant with 3-bromo-1,1,1-trifluoroacetone (BTFA). The 5FW and BTFA modifications cause minimal structural perturbation. Resonances from the 275 kDa complexes of sMMOH with 5FW-MMOB and BTFAK15C-5FW-MMOB are readily detected at 5 microM labeled protein concentration. This approach shows directly that MMOR and MMOB competitively bind to sMMOH with similar KD values, independent of the oxidation state of the sMMOH diiron cluster
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Colby, J.; Stirling, D.I.; Dalton, H.
The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate n-alkanes, n-alkenes, ethers, and alicyclic, aromatic and heterocyclic compounds
Biochem. J.
165
395-402
1977
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Tonge, G.M.; Harrison, D.E.F.; Higgins, I.J.
Purification and properties of the methane mono-oxygenase enzyme system from Methylosinus trichosporium OB3b
Biochem. J.
161
333-344
1977
Methylosinus trichosporium
brenda
Stirling, D.I.; Dalton, H.
Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath)
Eur. J. Biochem.
96
205-212
1979
Methylococcus capsulatus, Methylosinus trichosporium, Methylococcus capsulatus Bath
brenda
Pilkington, S.J.; Dalton, H.
Soluble methane monooxygenase from Methylococcus capsulatus Bath
Methods Enzymol.
188
181-190
1990
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
brenda
Fox, B.G.; Froland, W.A.; Jollie, D.R.; Lipscomb, J.D.
Methane monooxygenase from Methylosinus trichosporium OB3b
Methods Enzymol.
188
191-202
1990
Methylosinus trichosporium
brenda
Pilkington, S.J.; Dalton, H.
Purification and characterization of the soluble methane monooxygenase from Methylosinus sporium 5 demonstrates the highly conserved nature of this enzyme in methanotrophs
FEMS Microbiol. Lett.
78
103-108
1991
Methylosinus sporium, Methylosinus sporium 5
-
brenda
Patel, R.N.; Savas, J.C.
Purification and properties of the hydroxylase component of methane monooxygenase
J. Bacteriol.
169
2313-2317
1987
Methylobacterium sp.
brenda
Lund, J.; Dalton, H.
Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath)
Eur. J. Biochem.
147
291-296
1985
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Green, J.; Prior, S.D.; Dalton, H.
Copper ions as inhibitors of protein C of soluble methane monooxygenase of Methylococcus capsulatus (Bath)
Eur. J. Biochem.
153
137-144
1985
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Green, J.; Dalton, H.
Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity
J. Biol. Chem.
260
15795-15801
1985
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Woodland, M.P.; Dalton, H.
Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath)
J. Biol. Chem.
259
53-59
1984
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Dalton, H.; Smith, D.D.S.; Pilkington, S.J.
Towards a unified mechanism of biological methane oxidation
FEMS Microbiol. Lett.
87
201-208
1990
Methylobacterium sp., Methylococcus capsulatus, Methylosinus trichosporium, Methylococcus capsulatus Bath
-
brenda
Fox, B.G.; Liu, Y.; Dege, J.E.; Lipscomb, J.D.
Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction
J. Biol. Chem.
266
540-550
1991
Methylosinus trichosporium
brenda
Rataj, M.J.; Kauth, J.E.; Donnelly, M.I.
Oxidation of deuterated compounds by high specific activity methane monooxygenase from Methylosinus trichosporium. Mechanistic implications
J. Biol. Chem.
266
18684-18690
1991
Methylosinus trichosporium
brenda
Fox, B.G.; Lipscomb, J.D.
Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph
Biochem. Biophys. Res. Commun.
154
165-170
1988
Methylosinus trichosporium
brenda
Colby, J.; Dalton, H.
Some properties of a soluble methane mono-oxygenase from Methylococcus capsulatus strain Bath
Biochem. J.
157
495-497
1976
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Green, J.; Dalton, H.
Substrate specificity of soluble methane monooxygenase. Mechanistic implications
J. Biol. Chem.
264
17698-17703
1989
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Colby, J.; Dalton, H.
Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath)
Biochem. J.
177
903-908
1979
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Colby, J.; Dalton, H.
Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein
Biochem. J.
171
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Methylococcus capsulatus, Methylococcus capsulatus Bath
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Methylococcus capsulatus, Methylomonas sp., Methylosinus trichosporium, Methylomonas sp. GYJ3, Methylococcus capsulatus HD6T
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Methylococcus capsulatus
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Methylosinus trichosporium OB3b (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562), Methylosinus trichosporium OB3b
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Methylosinus trichosporium
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Methylosinus trichosporium OB3b (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562), Methylosinus trichosporium OB3b
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Methylococcus capsulatus, Methylococcus capsulatus Bath
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Methylococcus capsulatus (P22869 and P18798 and P11987 and P18797 and P22868 and P22867), Methylococcus capsulatus, Methylococcus capsulatus Bath. (P22869 and P18798 and P11987 and P18797 and P22868 and P22867)
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Castillo, R.G.; Banerjee, R.; Allpress, C.J.; Rohde, G.T.; Bill, E.; Que, L.; Lipscomb, J.D.; DeBeer, S.
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Methylosinus trichosporium (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562)
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Methylococcus capsulatus, Methylococcus capsulatus (P22869 and P18798 and P11987 and P18797 and P22868 and P22867), Methylococcus capsulatus Bath, Methylococcus capsulatus Bath. (P22869 and P18798 and P11987 and P18797 and P22868 and P22867)
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Methylosinus trichosporium (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562)
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Methylococcus capsulatus (P22869 and P18798 and P11987 and P18797 and P22868 and P22867), Methylosinus trichosporium (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562), Methylococcus capsulatus Bath. (P22869 and P18798 and P11987 and P18797 and P22868 and P22867)
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Nguyen, N.L.; Yu, W.J.; Yang, H.Y.; Kim, J.G.; Jung, M.Y.; Park, S.J.; Roh, S.W.; Rhee, S.K.
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Methylomonas sp. (A0A250DUW2), Methylomonas sp. EMGL16-1 (A0A250DUW2)
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Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases
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Methylococcus capsulatus, Methylococcus capsulatus (P22869 and P18798 and P11987 and P18797 and P22868 and P22867), Methylococcus capsulatus Bath, Methylococcus capsulatus Bath. (P22869 and P18798 and P11987 and P18797 and P22868 and P22867)
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Zhang, S.; Karthikeyan, R.; Fernando, S.
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Methylococcus capsulatus, Methylosinus trichosporium (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562), Methylococcus capsulatus Bath
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Structural Studies of the Methylosinus trichosporium OB3b soluble methane monooxygenase hydroxylase and regulatory component complex reveal a transient substrate tunnel
Biochemistry
59
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2020
Methylosinus trichosporium (A0A2D2D5X0 AND A0A2D2D0T8 AND Q53563 AND A0A2D2D0X7), Methylosinus trichosporium
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Soluble methane monooxygenase component interactions monitored by 19F NMR
Biochemistry
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Methylosinus trichosporium (A0A2D2D5X0 AND A0A2D2D0T8 AND Q53563 AND A0A2D2D0X7)
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X-ray crystal structures of methane monooxygenase hydroxylase complexes with variants of its regulatory component correlations with altered reaction cycle dynamics
Biochemistry
61
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2022
Methylosinus trichosporium (A0A2D2D5X0 AND A0A2D2D0T8 AND Q53563 AND A0A2D2D0X7)
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Methylosinus trichosporium (A0A2D2D5X0 AND A0A2D2D0T8 AND Q53563 AND A0A2D2D0X7)
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Yamamoto, T.; Hasegawa, Y.; Iwaki, H.
Identification and characterization of a novel class of self-sufficient cytochrome P450 hydroxylase involved in cyclohexanecarboxylate degradation in Paraburkholderia terrae strain KU-64
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Paraburkholderia terrae, Paraburkholderia terrae KU-64
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Methylosinus sporium, Methylosinus sporium 5, Methylosinus sporium ATCC 35069
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Lettau, E.; Zill, D.; Spaeth, M.; Lorent, C.; Singh, P.K.; Lauterbach, L.
Catalytic and spectroscopic properties of the halotolerant soluble methane monooxygenase reductase from Methylomonas methanica MC09
ChemBioChem
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Methylomonas methanica, Methylomonas methanica MC09
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High-resolution XFEL structure of the soluble methane monooxygenase hydroxylase complex with its regulatory component at ambient temperature in two oxidation states
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Methylosinus trichosporium (A0A2D2D5X0 AND A0A2D2D0T8 AND Q53563 AND A0A2D2D0X7)
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Methylosinus trichosporium (A0A2D2D5X0 AND A0A2D2D0T8 AND Q53563 AND A0A2D2D0X7)
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Methylosinus sporium, Methylosinus sporium 5, Methylosinus sporium ATCC 35069
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