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Literature summary for 1.14.18.3 extracted from

  • Cao, L.; Caldararu, O.; Rosenzweig, A.C.; Ryde, U.
    Quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase (2018), Angew. Chem. Int. Ed. Engl., 57, 162 -166 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ absolutely required, quantum refinement does not support dinuclear copper sites in crystal structures of particulate methane monooxygenase, copper content and binding structure analysis, crystal structures analysis from PDB IDs 3RGB and 3RFR, and modeling, QM-refined structures, detailed overview. Putative mechanism for the reaction of the mononuclear site with methane Methylococcus capsulatus
Zn2+ one Zn2+ ion is bound per enzyme molecule Methylococcus capsulatus

Organism

Organism UniProt Comment Textmining
Methylococcus capsulatus G1UBD1 AND Q607G3 alpha- and beta-subunits
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Methylococcus capsulatus Bath G1UBD1 AND Q607G3 alpha- and beta-subunits
-

Reaction

Reaction Comment Organism Reaction ID
methane + quinol + O2 = methanol + quinone + H2O putative mechanism for the reaction of the mononuclear site with methane, structure modeling, overview Methylococcus capsulatus

Synonyms

Synonyms Comment Organism
membrane-bound methane monooxygenase
-
Methylococcus capsulatus
particulate methane monooxygenase
-
Methylococcus capsulatus
pMMO
-
Methylococcus capsulatus

General Information

General Information Comment Organism
physiological function particulate methane monooxygenase (pMMO) can activate methane Methylococcus capsulatus