Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
- 1 December 1993
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 366 (6455), 537-543
- https://doi.org/10.1038/366537a0
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.Keywords
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