Methane monooxygenase

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(New page: <StructureSection load='1fz8' size='340' side='right' caption='Structure of methane monooxygenase α+β+γ subunits complex with Fe and dibromomethane (PDB code 1fz8). ' scene=''> ==...)
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<StructureSection load='1fz8' size='340' side='right' caption='Structure of methane monooxygenase α (grey and green) +β (pink and yellow) +γ (magenta and cyan) subunits complex with Fe+3 (red), Ca+2 (green) and dibromomethane (PDB code [[1fz8]]). ' scene=''>
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<StructureSection load='1fz8' size='340' side='right' caption='Structure of methane monooxygenase α+β+γ subunits complex with Fe and dibromomethane (PDB code [[1fz8]]). ' scene=''>
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== Function ==
== Function ==
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'''Methane monooxygenase''' (MMO) catalyzes the oxidation of the C-H bond of methane and other alkanes. MMO catalyzes the conversion of CH4 and O2 to CH3OH and H2O using NADPH as reducing agent. The soluble MMO (sMMO) has Fe-O-Fe in its active site while the particulate MMO (pMMO) has Cu in it. MMO is composed of 3 subunits. Subunit α is the hydroxylase and contains the di-iron active site. Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex. Subunit γ which is involved in coupling. MMO is found in methanotropic bacteria.
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'''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 />
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* Subunit α is the hydroxylase (MMOH) and contains the di-iron active site.<br />
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== Disease ==
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* Subunit β is a reductase which contains the co-factors FAD and 2Fe-2S complex.<br />
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* Subunit γ is regulatory (MMOR) and is involved in coupling.<br />
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== Relevance ==
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MMO is found in methanotropic bacteria.
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== Structural highlights ==
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==3D structures of methane monooxygenase==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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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 />
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[[1xmf]] – McMMO α+β+γ subunits + Mn<br />
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[[1xmh]] – McMMO α+β+γ subunits + Co<br />
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[[1xmg]] – McMMO α+β+γ subunits <br />
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[[1mhy]], [[1mhz]] – MtMMO α+β+γ subunits + Fe – ''Methylosinus trichosporium''<br />
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===sMMO complexes===
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[[1fz8]] – McMMO α+β+γ subunits + Fe + dibromomethane<br />
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[[1xvc]] – McMMO α+β+γ subunits + Fe + bromoethane + bromopentane <br />
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[[1xvb]] – McMMO α+β+γ subunits + Fe + bromoethane + bromopropane + bromobutane + bromohexanol <br />
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[[1fz9]] – McMMO α+β+γ subunits + Fe + iodoethane<br />
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[[1xvd]] – McMMO α+β+γ subunits + Fe + fluorophenol<br />
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[[1xve]] – McMMO α+β+γ subunits + Fe + bromobutenol<br />
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[[1xvf]] – McMMO α+β+γ subunits + Fe + chloropropanol<br />
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[[1xvg]] – McMMO α+β+γ subunits + Fe + bromoethanol<br />
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[[1xu3]] – McMMO α+β+γ subunits + Fe + bromophenol<br />
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[[4gam]] – McMMO α+β+γ subunits + Fe + MMO regulatory protein B<br />
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===sMMO γ subunit (MMO reductase, MMOR)===
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== Methane monooxygenase 3D structures==
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[[1jqr]] – McMMOR N terminal + Fe2S2 - NMR<br />
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[[Methane monooxygenase 3D structures]]
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[1tvc]] – McMMOR C terminal + FAD derivative - NMR<br />
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</StructureSection>
== References ==
== References ==

Current revision

Structure of methane monooxygenase α (grey and green) +β (pink and yellow) +γ (magenta and cyan) subunits complex with Fe+3 (red), Ca+2 (green) and dibromomethane (PDB code 1fz8).

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel

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