Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase.

Ramakrishnan Balasubramanian, Amy C Rosenzweig

Journal: Accounts of chemical research 2007;40(7):573-80

PMID: 17444606

Full Text on American Chemical Society View on PubMed

Abstract

Particulate methane monooxygense (pMMO) is an integral membrane copper-containing enzyme that converts methane to methanol. Knowledge of how pMMO selectively oxidizes methane under ambient conditions could impact the development of new catalysts. The crystal structure of Methylococcus capsulatus (Bath) pMMO reveals the composition and location of three metal centers. Spectroscopic data provide insight into the coordination environments and oxidation states of these metal centers. These results, combined with computational studies and comparisons to relevant systems, are discussed in the context of identifying the most likely site for O 2 activation.

Address: Department of Biochemistry, Northwestern University, Evanston, Illinois 60208, USA.

DOI: 10.1021/ar700004s

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MeSH Terms: Binding Sites, Computational Biology, Copper, Crystallography, X-Ray, Methane, Methylococcus capsulatus, Models, Molecular, Oxidation-Reduction, Oxygen, Oxygenases, Structure-Activity Relationship