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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasm | - |
Methylococcus capsulatus | 5737 | - |
cytoplasm | - |
Methylosinus trichosporium | 5737 | - |
soluble | - |
Methylococcus capsulatus | - |
- |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + NADH + H+ + O2 | Methylococcus capsulatus | - |
methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | Methylosinus trichosporium | - |
methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | Methylococcus capsulatus Bath | - |
methanol + NAD+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methylococcus capsulatus | - |
- |
- |
Methylococcus capsulatus Bath | - |
- |
- |
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) | - |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methane + NADH + H+ + O2 | - |
Methylococcus capsulatus | methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | - |
Methylosinus trichosporium | methanol + NAD+ + H2O | - |
? | |
methane + NADH + H+ + O2 | - |
Methylococcus capsulatus Bath | methanol + NAD+ + H2O | - |
? |
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 | Comment | Organism |
---|---|---|
sMMO | - |
Methylococcus capsulatus |
sMMO | - |
Methylosinus trichosporium |
soluble methane monooxygenase | - |
Methylococcus capsulatus |
soluble methane monooxygenase | - |
Methylosinus trichosporium |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 25 | - |
Methylosinus trichosporium |
37 | - |
- |
Methylococcus capsulatus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | 7 | - |
Methylosinus trichosporium |
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 | - |
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 | - |
Methylococcus capsulatus |
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 |