The particulate methane monooxygenase (pMMO) is the first enzyme in the C1 metabolic pathway in methanotrophic bacteria. As this enzyme converts methane into methanol efficiently near room temperature, it has become the paradigm for developing an understanding of this difficult C1 chemistry. pMMO is a membrane-bound protein with three subunits (PmoB, PmoA, and PmoC) and 12-14 coppers distributed among different sites. X-ray crystal structures that have revealed only three mononuclear coppers at three sites have neither disclosed the location of the active site nor the catalytic mechanism of the enzyme. Here you have a cyro-EM structure of holo -pMMO from Methylococcus capsulatus (Bath) at 2.5 Å (PDB code: 7EV9)
#molecularart ... #immolecular ... #methane ... #monooxygenase ... #particulated ... #enzyme ... #CryoEM ... Rendered with @proteinimaging and finished with @corelphotopaint
#molecularart ... #immolecular ... #methane ... #monooxygenase ... #particulated ... #enzyme ... #CryoEM ... Rendered with @proteinimaging and finished with @corelphotopaint
