Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

Raquel L. Lieberman, Amy C. Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticle

419 Scopus citations

Abstract

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 Å. The enzyme is a trimer with an α3β 3γ3 polypeptide arrangement. Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. A third metal centre, occupied by zinc in the crystal, is located within the membrane. The structure provides new insight into the molecular details of biological methane oxidation.

Original languageEnglish (US)
Pages (from-to)177-182
Number of pages6
JournalNature
Volume434
Issue number7030
DOIs
StatePublished - Mar 10 2005

ASJC Scopus subject areas

  • General

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