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.

摘要

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.CAS Registry/EC Number/Name of Substance 0 (Butanes). 0 (Butanols). 0 (Pentanes). 0 (Pentanols). 106-97-8 (butane). 109-66-0 (pentane). 78-92-2 (2-butanol). EC 1-13 (Oxygenases). EC 1-14-13-25 (methane monooxygenase).