Particulate methane monooxygenase contains only mononuclear copper centers

Matthew O. Ross(Northwestern University), Fraser MacMillan(University of East Anglia), Jingzhou Wang(California Institute of Technology), Alex Nisthal(California Institute of Technology), Thomas J. Lawton(Northwestern University), Barry D. Olafson(Protabit (United States)), Stephen L. Mayo(California Institute of Technology), Amy C. Rosenzweig(Northwestern University), Brian M. Hoffman(Northwestern University)
Science
May 9, 2019
Cited by 295Open Access
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Abstract

How many metals to oxidize methane? Methane is an important fuel, but there are few direct transformations to partially oxidized products. Bacteria use metalloenzymes to catalyze methane oxidation to methanol, a reaction of industrial interest. Understanding the metal sites that enable this reaction may inspire new biomimetic catalysts. Ross et al. used spectroscopic measurements to assign two monocopper sites in the enzyme particulate methane monooxygenase. These results differ in part from previous proposals for the location and nuclearity of the metal sites and will prompt rethinking about how this metalloenzyme catalyzes methane oxidation. Science , this issue p. 566


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