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={Amy C. Rosenzweig and Christin A. Frederick and Stephen J Lippard and P{\"a}r 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
Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
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The structure of pMMO is determined from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 Å and provides new insight into the molecular details of biological methane oxidation. Expand
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Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states.
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The diiron center in Hox can change its exogenous ligand coordination and geometry, a property that could be important in the catalytic cycle of sMMO. Expand
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TLDR
A structural model for the proposed catalytic site of the alternative oxidase of plant mitochondria is developed based on conserved amino acids that suggest the presence of a hydroxo‐bridged binuclear iron center, analogous to that found in the enzyme methane monooxygenase. Expand
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