New findings about Q

MPI CEC employees publish in JACS

Due to the diverse applications of methanol, whether as a fuel source, fuel additive or for power generation via fuel cells, it is of scientific and industrial interest to develop economical and sustainable methods for the production of industrial quantities.

The enzyme methane monooxygenase (MMO) catalyzes the oxidation of methane to methanol. In nature, two variants of this enzyme exist. The soluble MMO (sMMO) features a diiron core in its active center, while the particulate MMO (pMMO) utilizes copper. While a detailed understanding of the structure of these enzymes in all of its catalytic states is crucial for an in-depth insight of the reaction mechanism, scientists have debated for years about the structure of the key intermediate Q in sMMO.

Rebeca Gómez Castillo, PhD student at the IMPRS RECHARGE, and Prof. Serena DeBeer, director of the department ‚Iorganic Spectroscopy’ at MPI CEC, in a collaborative effort with the research groups of Prof. Lawrence Que Jr. and Prof. John D. Lipscomb of University of Minnesota, performed a detailed study on the controversial structure of the active site of intermediate Q.

This research was based on the local technique Kα HERFD-XAS (high energy resolution fluorescence detected X-ray absorption near edge structure), a powerful tool that overcomes the limitations of conventional x-ray absorption spectroscopy. When compared with synthetic model complexes spectra and supported by quantum chemical calculations, the analysis of the Kα HERFD-XAS data provides valuable information for clarifying the controversial structure of intermediate Q.

The study is published in the Journal of the American Chemical Society (JACS).

Find the publication in JACS:

High-Energy-Resolution Fluorescence-Detected X-ray Absorption of the Q Intermediate of Soluble Methane Monooxygenase

J. Am. Chem. Soc., Article ASAP DOI: 10.1021/jacs.7b09560

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