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

Amy C. Rosenzweig, Christin A. Frederick, Stephen J. Lippard*, Pär Nordlund

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

810 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)537-543
Number of pages7
JournalNature
Volume366
Issue number6455
DOIs
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • General

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