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

Abstract

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. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z604647_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.