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

@article{Rosenzweig1993CrystalSO,
  title={Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane},
  author={A. Rosenzweig and C. A. Frederick and S. Lippard and P. Nordlund},
  journal={Nature},
  year={1993},
  volume={366},
  pages={537-543}
}
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… Expand
Di-iron-carboxylate proteins.
Structure of the soluble methane monooxygenase regulatory protein B.
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