Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.
The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric hydroxylase protein of methane monooxygenase 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 alpha beta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis.
Rosenzweig
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Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Frederick
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Lippard
S J
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Nordlund
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D000595:Amino Acid Sequence; D001665:Binding Sites; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry; D007501:Iron / Q000032:analysis; D046911:Macromolecular Substances; D008697:Methane / Q000378:metabolism*; D008772:Methylococcaceae / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D010105:Oxygenases; C021555:methane monooxygenase; D008697:Methane