Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.
Rosenzweig, A.C., Frederick, C.A., Lippard, S.J., Nordlund, P.(1993) Nature 366: 537-543
- PubMed: 8255292 
- DOI: https://doi.org/10.1038/366537a0
- Primary Citation of Related Structures:  
1MMO - PubMed Abstract: 
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.
Organizational Affiliation: 
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.