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Monooxygenases
The Ohlendorf lab has determined the structure of methane monooxygenase hydroxylase (MMOH) from Methylosinus trichosporium OB3b. This 249,000 dalton dimer consists of three polypeptide chains that fold into the largely helical structure shown below. MMOH catalyzes the insertion of an atom of oxygen in a wide variety of carbon-hydrogen bonds. In name methane monooxygenase is used to capture 99.5% of the 109 tons of methane produce in oceans, lakes and wetlands annually by anaerobic fermentation and return it to biomass. MMOH is the catalytically competent subunit of methane monooxygenase.

Work on MMOH is in collaboration with Dr. John Lipscomb of the Dept. of Biochemistry of the University of Minnesota.

Schematic illustrating the secondary structure elements of the MMOH monomer. The biologically-active form of the molecule is the dimer.

Chime picture of MMOH.

 
Selected Publications
  • Elango, N., R. Radhakrishnan, et al. (1997). “Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b.” Protein Sci 6(3): 556-68.
  • Froland, W. A., D. H. Dyer, et al. (1994). “Preliminary crystallographic analysis of methane mono-oxygenase hydroxylase from Methylosinus trichosporium OB3b.” J Mol Biol 236(1): 379-81.