1.14.13.25: methane monooxygenase (soluble)
This is an abbreviated version!
For detailed information about methane monooxygenase (soluble), go to the full flat file.
Word Map on EC 1.14.13.25
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1.14.13.25
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methanotrophs
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methanol
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methylosinus
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capsulatus
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methylococcus
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trichosporium
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methane-oxidizing
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methylocystis
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ch4
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methylomonas
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dioxygen
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dinuclear
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methylobacter
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trichloroethylene
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methylomicrobium
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alkane
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diironii
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ammonia-oxidizing
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landfill
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upland
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antiferromagnetically
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wetland
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high-valent
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non-motile
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copper-containing
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carboxylate-bridged
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peat
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copper-dependent
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dicopper
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ch3oh
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nitrosomonas
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cometabolic
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diferrous
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methanobactins
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energy production
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mixed-valent
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gammaproteobacterial
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sphagnum
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t-rflp
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seep
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propene
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synthesis
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biotechnology
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degradation
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exafs
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nitrify
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peroxo
- 1.14.13.25
- methanotrophs
- methanol
- methylosinus
- capsulatus
- methylococcus
- trichosporium
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methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
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dinuclear
- methylobacter
- trichloroethylene
- methylomicrobium
- alkane
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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
Reaction
Synonyms
chcA, cytoplasmic methane monooxygenase, methane hydroxylase, methane mono-oxygenase, methane monooxygenase, methane monooxygenase hydroxylase, MmMmoC, MMO, MMO Bath, MMOB, MmoC, MMOH, MMOR, oxygenase, methane mono-, particulate methane monooxygenase, pMMO, sMMO, soluble methane monooxygenase, soluble methane monooxygenase hydroxylase
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Metals Ions
Metals Ions on EC 1.14.13.25 - methane monooxygenase (soluble)
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copper
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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, 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+
Fe
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
NaCl
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as a true halotolerant enzyme, MmoC still shows 50% of its specific activity at 2 M NaCl. Evaluation of salt tolerance for NADH-mediated reduction of benzyl viologen by MmoC at non-optima conditions, 23°C and pH 7.0
Zn2+
additional information
Cu2+
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copper genetically regulates the enzyme activity of the soluble and membrane-bound form
Cu2+
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cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Cu2+
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cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Cu2+
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copper-containing protein component contains one copper atom per molecule
Cu2+
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cytochrome component contains 0.3-0.8 atoms copper per molecule
Cu2+
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the membrane-bound pMMO contains 4.8 Cu2+ ions per 100 kDa protomer the purified pMMO contains 1.4 Cu2+ ions per 100 kDa protomer, the enzyme contains a dinuclear copper center
Cu2+
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cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)
Cu2+
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expression of the genes encoding sMMO and pMMO is regulated by copper ions, with sMMO expressed solely when copper is limiting
Cu2+
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when allylthiourea is removed, sMMO activity is maintained for an additional 24 generations, albeit at a slightly lower level due to the presence of 0.0007 mM of Cu2+ in the feed medium
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structural comparison of the di-iron center of MMOH (PDB ID 1MHY), MMOH-MMOB (PDB ID 4GAM), and MMOH-MMOD. Conformational changes in the MMOH four-helix bundle (helices B, C, E, and F) upon MMOB and MMOD binding. Six residues that coordinate to the two iron atoms are distributed on to the different helices
Fe
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the presence of iron at the diiron active site is required for the catalytic activity of the sMMO
Fe
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
the enzyme uses a nonheme, oxygen-bridged dinuclear iron cluster in the active site
Fe
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
the sMMOH active site contains a dinuclear iron cluster, which serves to activate molecular oxygen for insertion into the C-H bond of methane
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MOOH contains 3.7-4.1 Fe atoms per dimer, binding structure and geometric configuration, EXAFS and Fourier transformation analysis, detailed overview
Fe2+
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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+
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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
Fe2+
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the enzyme contains a Fe2S2 cluster, a bis-my-hydroxo-bridged dinuclear iron cluster, that binds to the enzyme reductase domain MMOR
Fe2+
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the purified pMMO contains 7.6 Fe2+ ions per 100 kDa protomer, the membrane-bound pMMO contains 2.1 Fe2+ ions per 100 kDa protomer
Fe2+
methylotrophic bacterium
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spin states in the polynuclear [Fe2O2] core cluster, a dinuclear oxygen-bridged iron(IV) model for the intermediate Q of the hydroxylase component of methane monooxygenase by means of spin-unrestricted KohnSham density functional theory, calculated coupling constants in calculation of Heisenberg coupling constants with Noodlemans Broken-Symmetry approach, computational method, optimized cluster structures, overview
Iron
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characterization of [Fe2-S2] redox centre of component C
Iron
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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
Iron
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non-heme iron, 3.02 mol iron per mol of enzyme, addition of exogenous FeCl2 or FeCl3 does not affect the enzyme activity
Iron
soluble methane monooxygenase consists of three subunits: a hydroxylase bridged with binuclear iron cluster, an NADH-dependent reductase component containing both flavin adenine dinucleotide (FAD) and ferredoxin [Fe2S2] cofactors, and regulatory protein which controls the reaction between the previous two. Low-temperature activation of methane is primarily achieved via Fe/Fe complex in the hydroxylase subunit. The Fe2S2 complex in soluble methane monooxygenase reductase only acts as a wired mediator to assist electron transport from the NAD/FAD redox couple to the di-iron complex in the hydroxylase. NAD and FAD simultaneously bind to a canyon region located midway between the two lobes in the reductase, forming a continuous wire, assisting the electron transport. The regulatory protein plays a vital role in helping the hydroxylase and reductase subunits to interface and causing conformational changes that control methane oxidation
Iron
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contains an Fe4+(micro-O)2Fe4+ center. A terminal hydroxo and a protonated His147 which is dissociated from a nearby Fe, is more asymmetric in its Fe(micro-O)2Fe diamond core, and is another very good candidate for intermediate Q
Iron
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in MmoH Fe-water distances vary from about 1.9 to 2.7 A, showing Fe1 to be 5 or 6 coordinate. The effect of binding toluene-4-monooxygenase D/MmoB to toluene-4-monooxygenase H/MmoH is not to remove a water ligand from either iron but to induce a change in orientation of the terminal glutamate on Fe2. This allows O2 to bridge the diiron site and aligns the redox active orbital on each Fe for efficient 2-electron transfer, facilitating the formation of a stabilized peroxo intermediate
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component A, hydroxylase component: contains 0.5 mol zinc per mol protein
Zn2+
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the purified pMMO contains 1.3 Zn2+ ions per 100 kDa protomer, the membrane-bound pMMO contains 2.7 Zn2+ ions per 100 kDa protomer
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sMMO activity and expression does not require Cu2+
additional information
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the enzyme does not contain and require Cu2+ for activity
additional information
the enzyme does not contain and require Cu2+ for activity
additional information
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the soluble methane monooxygenase contains no copper
additional information
the soluble methane monooxygenase contains no copper
additional information
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the enzyme contains very low or no amounts of copper and zinc
additional information
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sMMO activity and expression does not require Cu2+