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Synthesis

Better Model Of Methanol Enzyme

December 24, 2007 | APPEARED IN VOLUME 85, ISSUE 52

Some bacteria rely on the enzyme methane monooxygenase (MMO) to convert methane into methanol. Now, a research team led by Lawrence Que Jr. of the University of Minnesota, Minneapolis, and Eckard Münck of Carnegie Mellon University has synthesized a new diiron complex that provides a better model for studying MMO's mechanism of action (Proc. Natl. Acad. Sci. USA, DOI: 10.1073/pnas.0708516105). MMO's soluble version reacts with O2 to yield a diiron(IV) intermediate, simply called Q, which is the species known to oxidize CH4. Que and coworkers previously proposed that Q has a diamond-shaped FeIV2O2 core, and they synthesized an FeIIIFeIVO2 complex as a model. In the new work, the researchers were able to oxidize this complex to FeIV2O2 (shown) by electrolysis. Reactivity differences between the diiron model and an iron complex with an FeIV=O center provide clues to understanding MMO activity, the scientists say, in particular pointing to a mechanism in which the FeIV2O2 ring opens to form a terminal FeV=O unit that reacts with CH4.

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