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INSTITUTE COLLOQUIUM ON LEARNING FROM NATURE TO DEVELOP A CATALYST FOR THE FACILE CONVERSION OF METHANE TO METHANOLS |
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IIT Bombay is organising Institute Colloquium on Tuesday, November 3, 2009. The details are as follows:
Speaker: Prof. Sunny Chang Emeritus Professor California Institute of Technology, USA
Topic: Learning from Nature to Develop a Catalyst for the Facile Conversion of Methane to Methanols
Date: Tuesday, November 3, 2009
Time & Venue : 4.30 pm, F. C. Kohli Auditorium
-------------------------------------------------------------------------------------------------- Abstract : The particulate methane monooxygenase (pMMO) is a membrane-bound enzyme that mediates the facile conversion of methane to methanol under ambient conditions of temperature and pressure. In this lecture, I shall summarize efforts to obtain the purified pMMO in high yields and high specific activity from the methanotrophic bacteria Methylococcus capsulatus (Bath) for structural and biochemical characterization (1). The pMMO is a multi-copper protein containing ~15 copper ions. The enzyme utilizes a unique tricopper cluster to activate dioxygen for “O-atom” transfer to small alkanes and alkenes. Both the hydroxylation and epoxidation proceed with total retention of configuration of the carbon centers oxidized. This novel O-atom transfer chemistry will be discussed within the context of the recent X-ray crystal structure of the enzyme (2). Based on this new chemistry, an effort is now in progress to develop an artificial catalyst for similar controlled oxidation of organic substrates, including the facile conversion of methane to methanol in the laboratory. Several trinuclear [CuICuICuI]3+ clusters have been synthesized that are capable of mediating facile O-atom insertion across C-C and C-H bonds when they become activated by dioxygen at room temperature (3). This chemistry mimics the mechanism of hydroxylation of small alkanes that has been implicated in the pMMO. These results will also be presented.
(1) Chan SI, Yu SSF. 2008. Controlled oxidation of hydrocarbons by the membrane- bound methane monoxygenase: The case for a tricopper cluster.Acc. Chem. Res. 41:969–979.
(2) Lieberman RL, Rosenzwig AC. 2005. Crystal structure of a membrane-bound metalloenzyme that catalyzes the biological oxidation of methane. Nature 434:177–182.
(3) Chen PPY, Yang RBG, Lee JCM, Chan SI. 2007. Facile O-atom insertion into C–C and C–H bonds by a trinuclear copper complex designed to harness a “singlet oxene.” Proc. Natl. Acad. Sci. USA 104:14570–14575.
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