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Literature summary for 1.14.13.25 extracted from

  • Zhang, S.; Karthikeyan, R.; Fernando, S.
    Low-temperature biological activation of methane structure, function and molecular interactions of soluble and particulate methane monooxygenases (2017), Rev. Environ. Sci. Biotechnol., 16, 611-623 .
No PubMed abstract available

Application

Application Comment Organism
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) Methylococcus capsulatus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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Methylococcus capsulatus 5737
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cytoplasm
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Methylosinus trichosporium 5737
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soluble
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Methylococcus capsulatus
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-

Metals/Ions

Metals/Ions Comment Organism Structure
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 Methylococcus capsulatus
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 Methylosinus trichosporium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methane + NADH + H+ + O2 Methylococcus capsulatus
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methanol + NAD+ + H2O
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?
methane + NADH + H+ + O2 Methylosinus trichosporium
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methanol + NAD+ + H2O
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?
methane + NADH + H+ + O2 Methylococcus capsulatus Bath
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methanol + NAD+ + H2O
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?

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus
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-
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Methylococcus capsulatus Bath
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-
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Methylosinus trichosporium P27353 and P27355 and P27354 and P27356 and Q53563 and Q53562 P27353 (alpha/MmoX), P27355 (gamma/MmoZ), P27354 (beta/MmoY), P27356 (MmoB), Q53563 (MmoC), Q53562 (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)
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Reaction

Reaction Comment Organism Reaction ID
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 Methylococcus capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methane + NADH + H+ + O2
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Methylococcus capsulatus methanol + NAD+ + H2O
-
?
methane + NADH + H+ + O2
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Methylosinus trichosporium methanol + NAD+ + H2O
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?
methane + NADH + H+ + O2
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Methylococcus capsulatus Bath methanol + NAD+ + H2O
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?

Subunits

Subunits Comment Organism
More 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 Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
sMMO
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Methylococcus capsulatus
sMMO
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Methylosinus trichosporium
soluble methane monooxygenase
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Methylococcus capsulatus
soluble methane monooxygenase
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Methylosinus trichosporium

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 25
-
Methylosinus trichosporium
37
-
-
Methylococcus capsulatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 7
-
Methylosinus trichosporium

Cofactor

Cofactor Comment Organism Structure
FAD
-
Methylococcus capsulatus
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 Methylosinus trichosporium
additional information the overall picture of the sMMO reductase reveals an electron pathway as NADH -> FAD -> [2Fe-2S] -> methane monohydroxylase (MMOH) Methylococcus capsulatus
NADH
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Methylococcus capsulatus
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 Methylosinus trichosporium
[2Fe-2S]-center
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Methylococcus capsulatus

General Information

General Information Comment Organism
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 Methylococcus capsulatus
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 Methylococcus capsulatus