(1) Department of Chemistry and Biochemistry, Numazu College of Technology, Ooka, Numazu, 410-8501, Japan;(2) Department of Bioengineering, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan
Abstract:
The role of iron and copper in particulate methane monooxygenase (pMMO) of Methylosinus trichosporium OB3b is described, and an overview of the enzyme's properties is presented. The pMMO from M. trichosporium OB3b was solubilized in the detergent n-dodecyl--D-maltoside and purified by chromatographic techniques. The enzyme consists of 0.9 iron atoms and 12.8 copper atoms per molecule. The iron site in pMMO may be mononuclear non-heme iron. Copper exists as either copper ion coupled to four nitrogen atoms and/or trinuclear copper cluster wherein copper ions are ferromagnetically coupled.