Low-molecular-weight analogues of the soluble methane monooxygenase (sMMO): from the structural mimicking of resting states and intermediates to functional models.
The active centre of sMMO contains a diiron core ligated by histidine and glutamate residues, which is capable of catalysing a remarkable reaction: the oxidation of methane with O(2) yielding methanol. This review describes the results of efforts to prepare low-molecular-weight analogues of this active site directing towards 1) the assignment of the spectroscopic signatures identified for certain intermediates of the sMMO catalytic cycle to structural features and 2) the synthesis of molecular compounds that can mimic the reactivity. The historical development of the model chemistry, which is subdivided into structural and functional mimicking, is illustrated and achievements reached so far are highlighted.
Siewert
Inke
I
Institut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor Str. 2, 12489 Berlin, Germany.
Limberg
Christian
C
D002384:Catalysis; D020134:Catalytic Domain; D005290:Ferric Compounds / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000737:chemistry*; D012995:Solubility
D005290:Ferric Compounds; D010105:Oxygenases; C021555:methane monooxygenase