Abstract
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 αβ pairs, which have many long α-helices, for possible docking of the reductase and coupling proteins required for catalysis.
Original language | English (US) |
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Pages (from-to) | 537-543 |
Number of pages | 7 |
Journal | Nature |
Volume | 366 |
Issue number | 6455 |
DOIs | |
State | Published - 1993 |
ASJC Scopus subject areas
- General