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

Nature volume 366, pages 537–543 (1993)Cite this article

Abstract

The 2.2 Å 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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Authors and Affiliations

  1. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Amy C. Rosenzweig & Stephen J. Lippard

  2. Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School and Dana Farber Cancer Institute, Boston, Massachusetts, 02115, USA

    Christin A. Frederick

  3. Department of Molecular Biology, Stockholm University, S-10691, Stockholm, Sweden

    P& auml;r Nordlund

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  1. Amy C. Rosenzweig
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  2. Christin A. Frederick
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  3. Stephen J. Lippard
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  4. P& auml;r Nordlund
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Rosenzweig, A., Frederick, C., Lippard, S. et al. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 366, 537–543 (1993). https://doi.org/10.1038/366537a0

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