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Title: Methane monooxygenase, models and mechanisms

Methane monooxygenase, MMO, is a protein system that coverts methane to methanol in the first metabolic step of methanotropic bacteria. The hydroxylation reaction occurs at a dinuclear iron center in the 250 kDa hydroxylase enzyme, which functions with two partner proteins, a reductase and a coupling protein. Electrons enter the reductase which when substrate is bound to the hydroxylas enzyme, feeds electrons into the dinuclear iron centers with the assistance of the coupling protein. Oxygen then reacts with the reduced form of the hydroxylase to afford methanol and water. Studies will be presented that help to define the structure of the diiron center in the hydroxylase and features of the catalytic mechanism. The reaction chemistry of dioxygen with a variety of known and new model complexes will also be described and compared to postulated steps in the mechanism of hydroxylation of the natural system.
Authors:
 [1]
  1. Massachusetts Institute of Technology, Cambridge, MA (United States)
Publication Date:
OSTI Identifier:
141113
Report Number(s):
CONF-930304--
TRN: 93:003688-0788
Resource Type:
Conference
Resource Relation:
Conference: 205. American Chemical Society national meeting, Denver, CO (United States), 28 Mar - 2 Apr 1993; Other Information: PBD: 1993; Related Information: Is Part Of 205th ACS national meeting; PB: 1951 p.
Publisher:
American Chemical Society, Washington, DC (United States)
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; 40 CHEMISTRY; METHANE; OXIDATION; OXYGENASES; BIOLOGICAL PATHWAYS; BIOCHEMICAL REACTION KINETICS; METHANOTROPHIC BACTERIA; BIOCHEMISTRY; CATALYTIC EFFECTS; CHEMICAL REACTIONS