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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 + 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
-
-
-
?
bromomethane + NAD(P)H + O2
?
-
-
-
-
?
bromomethane + NADH + H+ + O2
?
-
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
-
?
carbon monoxide + NADH + H+ + O2
?
-
-
-
-
?
chloromethane + NAD(P)H + O2
formaldehyde + NAD(P)+ + H2O + ?
-
-
-
?
chloromethane + NADH + H+ + O2
?
-
-
-
-
?
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
-
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
dichloromethane + NAD(P)H + O2
CO + Cl- + NAD(P)+ + H2O
-
-
-
?
diethyl ether + NAD(P)H + O2
ethanol + ethanal + NAD(P)+ + H2O
-
-
-
?
difluoromethane + NADH + O2
difluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
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
ethene + NAD(P)H + O2
epoxyethane + NAD(P)+ + H2O
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
hexane + NAD(P)H + O2
1-hexanol + 2-hexanol + NAD(P)+ + 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
-
-
-
-
?
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 + O2
alpha-naphthol + beta-naphthol + NAD(P)+ + H2O
naphthalene + NADH + H+
alpha-naphthol + beta-naphthol + 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 + NAD(P)H + O2
propylene oxide + NADP+ + H2O
-
enzyme form sMMO
-
?
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
benzyl alcohol + p-cresol + NAD(P)+ + H2O
-
-
-
?
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
?
-
-
-
-
?
additional information
?
-
benzene + NAD(P)H + H+ + O2
phenol + hydroquinone + NAD(P)+ + H2O
-
-
-
?
benzene + NAD(P)H + H+ + O2
phenol + hydroquinone + 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
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + NAD(P)+ + H2O
-
-
-
?
cyclohexane + NAD(P)H + O2
cyclohexanol + 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
-
-
-
?
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
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + NAD(P)+ + H2O
-
-
-
?
heptane + NAD(P)H + O2
1-heptanol + 2-heptanol + 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
-
-
-
-
?
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 + 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 + 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
-
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
-
-
?
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
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + NAD(P)+ + H2O
-
-
-
?
pentane + NAD(P)H + O2
1-pentanol + 2-pentanol + 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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
?
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copper
-
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
Fe3+
the enzyme has diiron (FeIII-FeIII) active sites where different types of hydrocarbons are oxidized through orchestrated hydroxylase, regulatory and reductase components for precise control of hydrocarbons, oxygen, protons, and electrons
Ni2+
-
protein B contains 0.04 mol Ni2+ per mol protein
Zn2+
-
0.2-0.5 mol zinc per mol protein
Cu2+
-
component C contains no copper
Cu2+
-
copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
-
cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Fe2+
-
MOOH contains 3.7-4.1 Fe atoms per dimer, binding structure and geometric configuration, EXAFS and Fourier transformation analysis, detailed overview
Fe2+
-
the [2Fe-2S] cofactor of MMOR is a one-electron carrier, the ferredoxin center must transfer two electrons sequentially to MMOH to reduce fully each diiron(III) hydroxylase active site, overview
Fe2+
contains a diiron center
Fe2+
enzyme sMMO contains a non-heme diiron active site
Fe2+
-
the Fe2S2 domain of the reductase protein transfers electrons to carboxylate-bridged di-iron centers in the hydroxylase component of sMMO, structure of the Fe2S2 (ferredoxin) domain of sMMO reductase, overview. The Fe2S2 cluster is a di-iron pair coordinated by the sulfur atoms of cysteine residues 42, 47, 50, and 82
Iron
-
1.3-1.5 atoms iron per molecule
Iron
-
1 mol of [2Fe-2S(S-Cys)4]centre per mol protein
Iron
-
characterization of [Fe2-S2] redox centre of component C
Iron
-
2.3 mol Fe per mol protein
Iron
-
protein A, hydroxylase component: contains a binuclear iron center
Iron
-
protein C, reductase component: contains 1 [Fe2-S2]
Iron
non-heme diiron active site in the alpha-subunit. 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
Iron
the diiron active site of each homodimer is located in the alpha subunit, and no other metal centers are present. The resting state active site (MMOHox) consists of two Fe(III) ions coordinated by Glu114, His147, and a solvent molecule (Fe1), and Glu209, Glu243, and His246 (Fe2). The iron ions are 3.1 A apart, coordinated in pseudooctahedral fashion and bridged by two solvent molecules as well as Glu144
additional information
-
sMMO activity and expression does not require Cu2+
additional information
-
the enzyme does not contain and require Cu2+ for activity
additional information
the enzyme does not contain and require Cu2+ for activity
additional information
-
the soluble methane monooxygenase contains no copper
additional information
the soluble methane monooxygenase contains no copper
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dimer
-
component D of sMMO: 2 * 12000, 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)
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
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
enzyme system consists of 3 protein components A, B, C
additional information
-
structure, review
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
-
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
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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
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, Methylococcus capsulatus Bath, Methylosinus trichosporium
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
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, Methylococcus capsulatus Bath, 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
461-468
1978
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Murrell, J.C.; Gilbert, B.; McDonald, I.R.
Molecular biology and regulation of methane monooxygenase
Arch. Microbiol.
173
325-332
2000
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylocystis sp., Methylomicrobium album, Methylomicrobium album BG8
brenda
Merkx, M.; Lippard, S.J.
Why orfY? Characterization of MMOD, a long overlooked component of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
J. Biol. Chem.
277
5858-5865
2002
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Lloyd, J.S.; Bhambra, A.; Murrell, J.C.; Dalton, H.
Inactivation of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath) by proteolysis can be overcome by a Gly to Gln modification
Eur. J. Biochem.
248
72-79
1997
Methylococcus capsulatus
brenda
Brandstetter, H.; Whittington, D.A.; Lippard, S.J.; Frederick, C.A.
Mutational and structural analyses of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath)
Chem. Biol.
6
441-449
1999
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Sazinsky, M.H.; Merkx, M.; Cadieux, E.; Tang, S.; Lippard, S.J.
Preparation and X-ray structures of metal-free, dicobalt and dimanganese forms of soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)
Biochemistry
43
16263-16276
2004
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Astier, Y.; Balendra, S.; Hill, H.A.; Smith, T.J.; Dalton, H.
Cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
Eur. J. Biochem.
270
539-544
2003
Methylococcus capsulatus
brenda
Beauvais, L.G.; Lippard, S.J.
Reactions of the diiron(IV) intermediate Q in soluble methane monooxygenase with fluoromethanes
Biochem. Biophys. Res. Commun.
338
262-266
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Ukaegbu, U.E.; Henery, S.; Rosenzweig, A.C.
Biochemical characterization of MmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase
Biochemistry
45
10191-10198
2006
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Rudd, D.J.; Sazinsky, M.H.; Lippard, S.J.; Hedman, B.; Hodgson, K.O.
X-ray absorption spectroscopic study of the reduced hydroxylases of methane monooxygenase and toluene/o-xylene monooxygenase: differences in active site structure and effects of the coupling proteins MMOB and ToMOD
Inorg. Chem.
44
4546-4554
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Gherman, B.F.; Lippard, S.J.; Friesner, R.A.
Substrate hydroxylation in methane monooxygenase: quantitative modeling via mixed quantum mechanics/molecular mechanics techniques
J. Am. Chem. Soc.
127
1025-1037
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Blazyk, J.L.; Gassner, G.T.; Lippard, S.J.
Intermolecular electron-transfer reactions in soluble methane monooxygenase: a role for hysteresis in protein function
J. Am. Chem. Soc.
127
17364-17376
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Beauvais, L.G.; Lippard, S.J.
Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers
J. Am. Chem. Soc.
127
7370-7378
2005
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Zhang, Y.; Xin, J.; Chen, L.; Xia, C.
The methane monooxygenase intrinsic activity of kinds of methanotrophs
Appl. Biochem. Biotechnol.
157
431-441
2009
Methylococcus capsulatus, Methylomonas sp., Methylosinus trichosporium, Methylomonas sp. GYJ3, Methylococcus capsulatus HD6T
brenda
Anthony, C.
A tribute to Howard Dalton and methane monooxygenase
Sci. Prog.
91
401-415
2008
Methylococcus capsulatus
brenda
Tinberg, C.E.; Lippard, S.J.
Oxidation reactions performed by soluble methane monooxygenase hydroxylase intermediates H(peroxo) and Q proceed by distinct mechanisms
Biochemistry
49
7902-7912
2010
Methylococcus capsulatus
brenda
Tinberg, C.E.; Lippard, S.J.
Dioxygen activation in soluble methane monooxygenase
Acc. Chem. Res.
44
280-288
2011
Methylococcus capsulatus (P22869 and P18798 and P11987)
brenda
Lee, S.J.; McCormick, M.S.; Lippard, S.J.; Cho, U.S.
Control of substrate access to the active site in methane monooxygenase
Nature
494
380-384
2013
Methylococcus capsulatus (P22869 and P18798 and P11987)
brenda
Wang, V.C.; Maji, S.; Chen, P.P.; Lee, H.K.; Yu, S.S.; Chan, S.I.
Alkane oxidation methane monooxygenases, related enzymes, and their biomimetics
Chem. Rev.
117
8574-8621
2017
Methylococcus capsulatus, Methylococcus capsulatus Bath
brenda
Wang, W.; Lippard, S.J.
Diiron oxidation state control of substrate access to the active site of soluble methane monooxygenase mediated by the regulatory component
J. Am. Chem. Soc.
136
2244-2247
2014
Methylococcus capsulatus (P22869 and P18798 and P11987 and P18797 and P22868 and P22867), Methylococcus capsulatus Bath. (P22869 and P18798 and P11987 and P18797 and P22868 and P22867)
brenda
Wang, W.; Iacob, R.E.; Luoh, R.P.; Engen, J.R.; Lippard, S.J.
Electron transfer control in soluble methane monooxygenase
J. Am. Chem. Soc.
136
9754-9762
2014
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)
brenda
Ross, M.O.; Rosenzweig, A.C.
A tale of two methane monooxygenases
J. Biol. Inorg. Chem.
22
307-319
2017
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)
brenda
Lee, S.J.
Hydroxylation of methane through component interactions in soluble methane monooxygenases
J. Microbiol.
54
277-282
2016
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)
brenda
Larsen, O.; Karlsen, O.A.
Transcriptomic profiling of Methylococcus capsulatus (Bath) during growth with two different methane monooxygenases
MicrobiologyOpen
5
254-267
2016
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)
brenda
Zhang, S.; Karthikeyan, R.; Fernando, S.
Low-temperature biological activation of methane structure, function and molecular interactions of soluble and particulate methane monooxygenases
Rev. Environ. Sci. Biotechnol.
16
611-623
2017
Methylococcus capsulatus, Methylococcus capsulatus Bath, Methylosinus trichosporium (P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562)
-
brenda