Methane monooxygenase (MMO) is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. Methane monooxygenase belongs to the class of oxidoreductase enzymes. There are two forms of MMO: the well-studied soluble form (sMMO) and the particulate form (pMMO). The active site in sMMO contains a di-iron center bridged by an oxygen atom (Fe-O-Fe), whereas the active site in pMMO utilizes copper. Structures of both proteins have been determined by X-ray crystallography; however, the location and mechanism of the active site in pMMO is still poorly understood and is an area of active research. The particulate methane monooxygenase and related ammonia monooxygenase are integral membrane proteins, occurring in methanotrophs and ammonia oxidisers, respectively, which are thought to be related. These enzymes have a relatively wide substrate specificity and can catalyse the oxidation of a range of substrates including ammonia, methane, halogenated hydrocarbons, and aromatic molecules. These enzymes are homotrimers composed of 3 subunits - A (InterPro: IPR003393), B (InterPro: IPR006833) and C (InterPro: IPR006980) and most contain two monocopper centers. Here you can see the intrincated network of parallel alpha-helices observed in the cryoEM structure of the pMMO enzyme from Methylococcus capsulatus str. Bath (PDB code: 7YZY)
#molecularart ... #immolecular ... #methane ... #monooxygenase ... #membrane ... #trimer ... #alphahelix ... #cryoem
Structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #methane ... #monooxygenase ... #membrane ... #trimer ... #alphahelix ... #cryoem
Structure rendered with @proteinimaging and depicted with @corelphotopaint
