Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b

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 solubil ized in the detergent n-dodecyl-beta -D-maltoside and purified by chromatog raphic techniques. The enzyme consists of 0.9 iron atoms and 12.8 copper at oms per molecule. The iron site in pMMO may be mononuclear non-heme iron. C opper exists as either copper ion coupled to four nitrogen atoms and/or tri nuclear copper cluster wherein copper ions are ferromagnetically coupled.