Methane monooxygenase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Methane monooxygenase''' (MMO) catalyzes the oxidation of the C-H bond of methane and other alkanes. MMO catalyzes the conversion of CH<sub>4</sub> and O<sub>2</sub> to CH<sub>3</sub>OH and H<sub>2</sub>O using NADPH as reducing agent. The '''soluble MMO (sMMO)''' has Fe-O-Fe in its active site<ref>PMID:7826011</ref> while the '''particulate MMO (pMMO)''' has Cu in it<ref>PMID:21419924</ref>. MMO is composed of 3 subunits.<br /> | + | '''Methane monooxygenase''' or '''Methane monooxygenase hydroxylase''' (MMO) catalyzes the oxidation of the C-H bond of methane and other alkanes. MMO catalyzes the conversion of CH<sub>4</sub> and O<sub>2</sub> to CH<sub>3</sub>OH and H<sub>2</sub>O using NADPH as reducing agent. The '''soluble MMO (sMMO)''' has Fe-O-Fe in its active site<ref>PMID:7826011</ref> while the '''particulate MMO (pMMO)''' has Cu in it<ref>PMID:21419924</ref>. MMO is composed of 3 subunits.<br /> |
| - | * Subunit α is the hydroxylase and contains the di-iron active site.<br /> | + | * Subunit α is the hydroxylase (MMOH) and contains the di-iron active site.<br /> |
* Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br /> | * Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br /> | ||
| - | * Subunit γ | + | * Subunit γ is regulatory (MMOR) and is involved in coupling.<br /> |
MMO is found in methanotropic bacteria. | MMO is found in methanotropic bacteria. | ||
| - | == | + | == Methane monooxygenase 3D structures== |
| - | + | [[Methane monooxygenase 3D structures]] | |
| - | == Structural highlights == | ||
</StructureSection> | </StructureSection> | ||
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| - | ==3D structures of methane monooxygenase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *'''Methane monooxygenase''' | ||
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| - | **[[1mmo]], [[1mty]], [[1fyz]], [[1fz0]], [[1fz1]], [[1fz2]], [[1fz3]], [[1fz4]], [[1fz5]], [[1fz6]], [[1fz7]], [[1fzh]], [[1fzi]], [[1xu5]] – McMMO α+β+γ subunits + Fe – ''Methylococcus capsulatus''<br /> | ||
| - | **[[1xmf]] – McMMO α+β+γ subunits + Mn<br /> | ||
| - | **[[1xmh]] – McMMO α+β+γ subunits + Co<br /> | ||
| - | **[[1xmg]] – McMMO α+β+γ subunits <br /> | ||
| - | **[[1yew]], [[3rgb]] – McMMO α+β+γ subunits + Cu + Zn<br /> | ||
| - | **[[1mhy]], [[1mhz]] – MtMMO α+β+γ subunits + Fe – ''Methylosinus trichosporium''<br /> | ||
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| - | *MMO complexes | ||
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| - | **[[1fz8]] – McMMO α+β+γ subunits + Fe + dibromomethane<br /> | ||
| - | **[[1xvc]] – McMMO α+β+γ subunits + Fe + bromoethane + bromopentane <br /> | ||
| - | **[[1xvb]] – McMMO α+β+γ subunits + Fe + bromoethane + bromopropane + bromobutane + bromohexanol <br /> | ||
| - | **[[1fz9]] – McMMO α+β+γ subunits + Fe + iodoethane<br /> | ||
| - | **[[1xvd]] – McMMO α+β+γ subunits + Fe + fluorophenol<br /> | ||
| - | **[[1xve]] – McMMO α+β+γ subunits + Fe + bromobutenol<br /> | ||
| - | **[[1xvf]] – McMMO α+β+γ subunits + Fe + chloropropanol<br /> | ||
| - | **[[1xvg]] – McMMO α+β+γ subunits + Fe + bromoethanol<br /> | ||
| - | **[[1xu3]] – McMMO α+β+γ subunits + Fe + bromophenol<br /> | ||
| - | **[[4gam]] – McMMO α+β+γ subunits + Fe + MMO regulatory protein B<br /> | ||
| - | **[[4phz]], [[4pi0]] – MeMMO α+β+γ subunits + Cu + peptide - ''methylocystis''<br /> | ||
| - | **[[4pi2]] – MeMMO α+β+γ subunits + Cu + Zn + peptide <br /> | ||
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| - | *MMO γ subunit (MMO reductase, MMOR) | ||
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| - | **[[1jqr]] – McMMOR N terminal + Fe2S2 - NMR<br /> | ||
| - | **[[1tvc]] – McMMOR C terminal + FAD derivative - NMR<br /> | ||
| - | }} | ||
== References == | == References == | ||
Current revision
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References
- ↑ Lipscomb JD. Biochemistry of the soluble methane monooxygenase. Annu Rev Microbiol. 1994;48:371-99. PMID:7826011 doi:http://dx.doi.org/10.1146/annurev.mi.48.100194.002103
- ↑ Miyaji A. Particulate methane monooxygenase from Methylosinus trichosporium OB3b. Methods Enzymol. 2011;495:211-25. doi: 10.1016/B978-0-12-386905-0.00014-0. PMID:21419924 doi:http://dx.doi.org/10.1016/B978-0-12-386905-0.00014-0
