Methane monooxygenase (MMO) is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. 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. Full activity of soluble methane monooxygenase (sMMO) depends upon the formation of a 1:1 complex of the regulatory protein MMOB with each alpha subunit of the (αβγ) 2 hydroxylase, sMMOH. Previous studies have shown that mutations in the core region of MMOB and in the N- and C-termini cause dramatic changes in the rate constants for steps in the sMMOH reaction cycle. Here you can see a side view of the x-ray structure of the methane monooxygenase hydroxylase and regulatory subunit DBL1 from Methylosinus trichosporium OB3b (PDB code: 7S6S)
#molecularart ... #immolecular ... #monoxygenase ... #methane ... #methylotrophic ... #hydrocarbon ... #energy ... #methylosinus ... #xray
Enzymatic complex structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #monoxygenase ... #methane ... #methylotrophic ... #hydrocarbon ... #energy ... #methylosinus ... #xray
Enzymatic complex structure rendered with @proteinimaging and depicted with @corelphotopaint
