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Article
Nature 366, 537 - 543 (09 December 1993); doi:10.1038/366537a0

Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane

Amy C. Rosenzweig& ast;, Christin A. Frederick& dagger;, Stephen J. Lippard& ast;& Dagger; & P& auml;r Nordlund& sect;& Dagger;

& ast;Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
& dagger;Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Dana Farber Cancer Institute, Boston, Massachusetts 02115, USA
& sect;Department of Molecular Biology, Stockholm University, S-10691 Stockholm, Sweden
& Dagger;To whom correspondence should be addressed.

The 2.2 & Aring; crystal structure of the 251K α2β2γ2 dimeric hydroxylase protein of methane mono-oxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between αβ pairs, which have many long α-helices, for possible docking of the reductase and coupling proteins required for catalysis.

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