Any feedback?
Information on EC 1.14.13.25 - methane monooxygenase (soluble) and Organism(s) Methylococcus capsulatus and UniProt Accession P11987
for references in articles please use BRENDA:EC1.14.13.25Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.13.25 methane monooxygenase (soluble)IUBMB Comments
The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO2, ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly.
Specify your search results
Word Map
- 1.14.13.25
- methanotrophs
- methanol
- methylosinus
- capsulatus
- methylococcus
- trichosporium
-
methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
-
dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
-
diironii
-
ammonia-oxidizing
-
landfill
-
upland
-
antiferromagnetically
-
wetland
-
high-valent
-
non-motile
-
copper-containing
-
carboxylate-bridged
-
peat
-
copper-dependent
-
dicopper
- ch3oh
- nitrosomonas
-
cometabolic
-
diferrous
-
methanobactins
- energy production
-
mixed-valent
-
gammaproteobacterial
- sphagnum
-
t-rflp
-
seep
- propene
- synthesis
- biotechnology
- degradation
-
exafs
-
nitrify
-
peroxo
The taxonomic range for the selected organisms is: Methylococcus capsulatus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
particulate methane monooxygenase, soluble methane monooxygenase, methane mono-oxygenase, methane monooxygenase hydroxylase, soluble methane monooxygenase hydroxylase, methane hydroxylase, cytoplasmic methane monooxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methane hydroxylase
-
-
-
-
methane mono-oxygenase
-
-
-
-
MMO
-
-
MMOH
oxygenase, methane mono-
-
-
-
-
pMMO
sMMO
soluble methane monooxygenase
MMOH
diiron(II) center of the hydroxylase component of soluble methane monooxygenase
sMMO
-
-
sMMO
the enzyme contains three protein components, a 251 kDa hydroxylase (MMOH), a 38.6 kDa reductase (MMOR), and a 15.9 kDa regulatory protein (MMOB) required to couple electron consumption with substrate hydroxylation at the catalytic diiron center of MMOH
sMMO
-
soluble methane monooxygenase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
mechanism
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
structural model for component protein B of sMMO
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
modeling of interaction between the different protein components of sMMO
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
distribution of electrons in intermolecular electron-transfer intermediates, isomerization of the initial ternary complex is required for maximal electron-transfer rates
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism via carboxylate-bridged diiron center and dioxygen, a di(my-oxo)diiron(IV) intermediate termed Q is responsible for the catalytic activity with hydrocarbons, the peroxodiiron(III) intermediate precedes Q formation in the catalytic cycle, which consists of four principal steps, overview
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
the soluble enzyme utilizes a carboxylate-bridged diiron center and dioxygen, a di(my-oxo)diiron(IV) intermediate termed Q is responsible for the catalytic activity with hydrocarbons, the peroxodiiron(III) intermediate precedes Q formation in the catalytic cycle
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
via diiron(IV) reaction intermediate Q, reaction mechanism of the soluble enzyme with different substrates, overview
-
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism and reaction cycle of enzyme sMMO, via O2 activation intermediates, detailed overview
methane + NAD(P)H + H+ + O2 = methanol + NAD(P)+ + H2O
reaction mechanism of enzyme sMMO. During methane oxidation, first, the regulatory protein docks at the alpha2beta2 interface of alpha2beta2gamma2 of hydroxylase and therefore triggering a conformational change in the alpha-subunit. Subsequently, the hydroxylase acts as a proton carrier allowing oxygen and methane interface with the di-iron center, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
methane,NAD(P)H:oxygen oxidoreductase (hydroxylating)
The enzyme is soluble, in contrast to the particulate enzyme, EC 1.14.18.3. Broad specificity; many alkanes can be hydroxylated, and alkenes are converted into the corresponding epoxides; CO is oxidized to CO2, ammonia is oxidized to hydroxylamine, and some aromatic compounds and cyclic alkanes can also be hydroxylated, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY
51961-97-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
beta-pinene + NAD(P)H + O2
6,6-dimethylbicyclo[3.1.1]hept-2-ene-2-methanol + beta-pinene oxide + NAD(P)+ + H2O
-
-
-
?
butane + NAD(P)H + O2
1-butanol + 2-butanol + NAD(P)+ + H2O
-
-
-
?
chloromethane + NAD(P)H + O2
formaldehyde + NAD(P)+ + H2O + ?
-
-
-
?
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
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
-
-
?
fluoromethane + NADH + O2
fluoromethanol + NAD+ + H2O
-
soluble enzyme
-
-
?
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 + NADH + H+
alpha-naphthol + beta-naphthol + NAD+ + H2O
-
-
-
-
?
octane + NAD(P)H + O2
1-octanol + 2-octanol + NAD(P)+ + H2O
-
-
-
?
phenylalanine + NAD(P)H + O2
tyrosine + NAD(P)+ + H2O
-
-
-
?
propane + NAD(P)H + O2
1-propanol + 2-propanol + NAD(P)+ + 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
-
-
-
?
pyridine + NAD(P)H + O2
pyridine N-oxide + NAD(P)+ + H2O
-
-
-
?
toluene + NAD(P)H + H+ + O2
benzyl alcohol + p-cresol + NAD(P)+ + H2O
-
-
-
?
trichloromethane + NAD(P)H + O2
CO2 + Cl- + 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
-
-
-
?
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
-
-
-
?
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
-
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 + 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
-
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
-
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
initial step in the assimilation of methane in bacteria that grow with methane as sole carbon and energy source
-
-
?
methane + reduced acceptor + H* + O2
methanol + acceptor + 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
-
-
?
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
?
-
-
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 sMMO enzyme has broad substrate specificity compared to pMMO
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview
-
FAD
-
protein C, reductase component: contains 1 mol FAD per mol protein
NADH
-
-
438920, 438922, 438928, 438929, 438930, 438931, 438932, 438936, 438937, 438938, 438939, 438943, 438945, 438949, 658051, 671722, 672049, 673999, 674145, 674158, 674170, 701759, 711260, 745389
additional information
-
component D contains no metal ions or organic cofactors
-
additional information
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
-
additional information
-
the overall picture of the sMMO reductase reveals an electron pathway as NADH -> FAD -> [2Fe-2S] -> methane monohydroxylase (MMOH)
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Cu2+
Fe2+
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
Iron
additional information
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+
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
-
characterization of [Fe2-S2] redox centre of component C
Iron
-
protein A, hydroxylase component: contains a binuclear iron center
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
poly-beta-hydroxybutyrate
-
MMO activity dramatically decreases when cellular poly-beta-hydroxybutyrate accumulates in the second stage. The more poly-beta-hydroxybutyrate are accumulated, the slower MMO activity decreases. Cellular poly-beta-hydroxybutyrate content has some influence on the maintenance of the MMO activity
protein MMOB
-
inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview
-
protein MMOD
-
inhibition of sMMO auxiliary proteins MMOB or MMOD severely diminishes electron-transfer throughput from MMOR, primarily by shifting the bulk of electron transfer to the slowest pathway, the biphasic reactions for electron transfer to MMOH from several MMOR ferredoxin analogues are also inhibited, overview
-
Cu2+
-
copper ions irreversibly inhibit the activity of sMMO in vivo and in vitro by inactivating the reductase component
additional information
-
sMMO is completely inhibited by monomeric component D, but not by dimeric, monomeric MMOD is interfering with the catalytically active complex between component A hydroxylase and component protein B
-
additional information
-
when cultivated in nutrients deficiency culture, activity of sMMO does not decrease
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
catalase
-
reduction current is enhanced by the presence of catalase ot if the reaction is performed in a flow-cell, probably because O2 is reduced to H2O2, by the hydroxylase component of the enzyme MMOH at the electrode surface and the H2O2 then inactivates the enzyme unless removed by catalase or a continous flow solution
-
regulatory protein MMOB
the native regulatory protein MMOB is required for maximum enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
analysis of kinetics of single turnover reactions of the two intermediates with ethyl vinyl ether and diethyl ether, single- and double-mixing stopped-flow optical spectroscopy, overview, stopped-flow kinetics, analytical model of transient kinetics
-
additional information
additional information
-
kinetics, deuterium kinetic isotope effects, overview
-
additional information
additional information
-
soluble enzyme, stopped-flow transient kinetics, double-mixing stopped-flow optical spectroscopic measurements, difluoromethane exhibits a smaller second-order rate constant for reaction with intermediate Q compared to methane
-
additional information
additional information
-
thermodynamics, stopped-flow kinetics, time-course profiles for MMOH reduction by MMOR ferredoxin and by MMOR3e-
-
additional information
additional information
-
kinetics for class III substrates of Hperoxo, and kinetics and thermodynamic parameters for class III substrates of Q at 4°C and 20°C, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
recombinant shows higher activity than the wild-type
additional information
-
quantitative modeling of substrate hydroxylation via mixed quantum mechanics/molecular mechanics techniques, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
45
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
438942, 658632, 671722, 672049, 673999, 674145, 674158, 674170, 701759, 706752, 711260, 744688, 745389, 745730, 746420
-
-
alpha subunit and beta subunit and gamma subunit
UniProt
Bath
438920, 438922, 438923, 438928, 438929, 438930, 438931, 438932, 438936, 438937, 438938, 438939, 438943, 438949, 658051
-
-
P22869 (MmoX), P18798 (MmoY), P11987 (MmoZ), P18797 (MmoB), P22868 (MmoC), P22867 (MmoD). The soluble methane monooxygenase (sMMO) consists of four components A/MMOH (composed of alpha/MmoX, beta/MmoY and gamma/MmoZ), B/MMOB (MmoB), C/MMOR (MmoC) and D/MMOD (MmoD)
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
transcriptomic profiling of soluble MMO is used to investigate the gene expression pattern in Methylococcus capsulatus during methanotrophic growth in the presence and absence of copper, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
-
enzyme from cells grown under conditions of low copper availability
-
cytoplasmatic, soluble enzyme form termed sMMO
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
metabolism
physiological function
additional information
metabolism
methane hydroxylation through methane monooxygenases is a key aspect due to their control of the carbon cycle in the ecology system
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
physiological function
-
pMMO consists of two protein components (NADH-OR and pMH) and is coupled to the electron transport chain
physiological function
-
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
-
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
additional information
-
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
-
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
42000
54000
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
additional information
17000
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
42000
-
component A: 2 * 54000 alpha + 2 * 42000 beta + 2 * 17000 gamma, SDS-PAGE and analytical ultracentrifugation
additional information
-
see under subunits: molecular weights of the subunits of components
additional information
-
see under subunits: molecular weights of the subunits of components
additional information
-
see under subunits: molecular weights of the subunits of 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
-
protein B shows unusual behaviour in gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
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
-
sMMO consists of 4 components: a hydroxylase, a reductase, a protein B and a protein D
additional information
-
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
-
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
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme sMMO crystal structure analysis, PDB ID 1MTY
sitting drop vapor diffusion method, using 0.1 M MES (pH 6.5) and 15% PEG 20000 (w/v)
X-ray crystal structure of the apo, Mn(II)-soaked, and Co(II)-grown hydroxylase component of methane monooxygenase, determined at 2.3 A or greater resolution, reveal that the presence of metal ions is essential for the proper folding of helices E, F, and H of the alpha-subunit
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G10A/G13Q/G16A
G13Q
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
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
-
enhanced temperature stability compared to wild-type, site-directed mutagenesis
G13Q
-
sMMO, alteration of a cleavage site in component protein B
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
5 mM thioglycollate, 5 mM dithiothreitol, 5 mM NADH stabilize component C at 0°C
-
protein B, in crude form requires addition of protease inhibitor phenylmethylsulfonyl fluoride
-
protein C requires presence of thiol protective agent, e.g. sodium thioglycolate throughout purification
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
component D of sMMO recombinant from Escherichia coli as His-tagged thioredoxin-fusion protein, the thioredoxin is cleaved off during purification by factor Xa
-
DEAE-Sepharose column chromatography, Q sepharose column chromatography, S-200 gel filtration, and S-300 gel filtration
native MMOH, in the purification procedure includes anion exchange chromatography and gel filtration
-
recombinant component protein B of sMMO as glutathione-S-transferase fusion protein from Escherichia coli
-
sMMO protein B wild-type and mutants recombinant from Escherichia coli by affinity chromatography, high salt concentration increases the binding stability between protein B and hydroxylase of sMMO
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression of component protein B of sMMO as glutathione-S-transferase fusion protein in Escherichia coli
-
expression of His-tagged triple mutant G10A/G13Q/G16A and G13Q mutant in Escherichia coli
-
overexpression of an additional protein component D of sMMO encoded by orfY as thioredoxin-fusion protein with His-Tag in Escherichia coli, protein component D is termed MMOD
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
activity of pMMO in whole cells is approximately 10fold greater than that of the purified sample
-
expressed in copper-limited conditions
the sMMO enzyme is expressed when cells are essentially starved for copper and the copper-to-biomass ratio is low (less than 0.0002 mM Cu2+)
-
transcription of sMMO is arrested in cells exposed to high levels of copper ions and sMMO mRNA transcripts are not detected 15 min after the addition of CuSO4
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
high particulate methane monooxygenase activity may contribute to the synthesis of poly-beta-hydroxybutyrate in the cell, which may be used to improve the yield of poly-beta-hydroxybutyrate in methanotrophs
energy production
-
teh enzyme can be used as biocatalysts for industrial activation of methane at relatively low temperatures required for breaking the highly stable C-H bond(s)
synthesis
-
cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode. The electrochemically driven enzyme shows the same catalytic activity and regulation by the protein component B (MMOB) as the natural NAD(P)H-driven reaction and may have the potential for development into economic NAD(P)H-independent oxygenation catalyst
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Pilkington, S.J.; Dalton, H.
Soluble methane monooxygenase from Methylococcus capsulatus Bath
Methods Enzymol.
188
181-190
1990
Methylococcus capsulatus, Methylococcus capsulatus Bath
-
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
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
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
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
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
-
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
Green, J.; Dalton, H.
Substrate specificity of soluble methane monooxygenase. Mechanistic implications
J. Biol. Chem.
264
17698-17703
1989
Methylococcus capsulatus, Methylococcus capsulatus Bath
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
Anthony, C.
A tribute to Howard Dalton and methane monooxygenase
Sci. Prog.
91
401-415
2008
Methylococcus capsulatus
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
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)
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)
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
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)
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)
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)
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)
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)
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)
-
EXTERNAL LINKS (specific for EC-Number 1.14.13.25)
Transporter Classification Database (TCDB): 9.B.280.1.1
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
