Abstract
The particulate methane monooxygenase (pMMO) of Methylosinus trichosporium OB3b oxidized n-butane and n-pentane and mainly produced (R)-2-butanol and (R)-2-pentanol that comprised 78 and 89% of the product, respectively, indicating that the pro-R hydrogen of the 2-position carbon of n-butane and n-pentane is oriented toward a catalytic site within the substrate binding site of pMMO. The protein cavity adjacent to the catalytic center for pMMO has optimum volume for recognizing n-butane and n-pentane for enantioselective hydroxylation.
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Acknowledgment
This work was supported by a Grant-in-Aid for Young Scientists (B) (No. 20760527, 23760739), from the Ministry of Education, Culture, Sports, Science and Technology, Japan, and partly by the Cooperative Research Program of Catalysis Research Center (CRC) Hokkaido University (Grant No. 10B2005). We thank Prof. Atsushi Fukuoka (CRC, Hokkaido University).
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Miyaji, A., Miyoshi, T., Motokura, K. et al. The substrate binding cavity of particulate methane monooxygenase from Methylosinus trichosporium OB3b expresses high enantioselectivity for n-butane and n-pentane oxidation to 2-alcohol. Biotechnol Lett 33, 2241–2246 (2011). https://doi.org/10.1007/s10529-011-0688-3
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DOI: https://doi.org/10.1007/s10529-011-0688-3