Redox Potentiometry Studies of Particulate Methane Monooxygenase: Support for a Trinuclear Copper Cluster Active Site

Authors


  • This work was supported by Academia Sinica as well as by a grant from the National Science Council (NSC94-2113-M-001-046).

Abstract

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A pocketful of coppers: Redox potentiometry and EPR experiments have confirmed that the active site of the particulate methane monooxygenase (pMMO), a membrane-bound enzyme that hydroxylates methane to methanol under ambient conditions, consists of one trinuclear copper cluster (see picture) and one type 2 copper site, in addition to the dinuclear copper cluster revealed previously by X-ray crystallography.

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