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
-
methane-oxidizing
- methylocystis
- ch4
- methylomonas
- dioxygen
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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
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
ECTree
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Cofactor
Cofactor on EC 1.14.13.25 - methane monooxygenase (soluble)
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cytochrome c
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one of three protein components is a soluble CO-binding cytochrome c
FAD
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protein C, reductase component: contains 1 mol FAD per mol protein
FAD
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protein C, reductase component: contains 1 mol FAD per mol protein
FAD
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protein C, reductase component: contains 1 mol FAD per mol protein
FAD
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
FAD
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the FAD-containing domain MMOR-FAD consits of MMOR residues 97-343
FAD
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the specific activity of MmoC is increased significantly by 20% in presence of 25 microM FAD, whereas addition of FMN does not improve activity confirming FAD as the prosthetic group
Ferredoxin
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several MMOR ferredoxin analogues, intermolecular electron transfer from ferredoxin analogues to hydroxylase protein MMOH, redox potential determinations, overview
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NADH
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NADH
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two-electron reduction of MMOHox by NADH mediated by MMOR enables further oxidation cycles
NADH
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
NADH
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NADH binds to the MMOR-FAD in MMOH to transfer hydride, and the conformational change of NADH-FAD generates charge transfer bands
[2Fe-2S]-center
A0A2D2D5X0; A0A2D2D0T8; Q53563; A0A2D2D0X7
in the 2Fe-2S cluster-containing reductase (MMOR)
additional information
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component D contains no metal ions or organic cofactors
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additional information
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cofactor-independent oxygenation reactions catalyzed by soluble methane monooxygenase at the surface of a modified gold electrode
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additional information
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the overall picture of the sMMO reductase reveals an electron pathway as NADH -> FAD -> [2Fe-2S] -> methane monohydroxylase (MMOH)
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additional information
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presence of a FAD and a [2Fe2S] cluster as its prosthetic group at the reductase MmoC component of the soluble methane monooxygenase complex. The MmMmoC prefers NADH instead of NADPH. No NADPH oxidation activity can be determined at 1 mM
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