Kato Shigeru, Yang Hui-Jun, Ueno Takafumi, Ozaki Shin-ichi, Phillips George N, Fukuzumi Shunichi, Watanabe Yoshihito
Department of Structural Molecular Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan.
J Am Chem Soc. 2002 Jul 24;124(29):8506-7. doi: 10.1021/ja0256414.
The H64D/V68A and H64D/V68S mutants of Myoglobin are found to oxidize thioanisole with high enantioselectivity and reactivity. These mutants are also capable of enantioselective binding of alpha-methylbenzylamine, which mimics an expected sulfoxidation intermediate. The kinetic study of the amine binding shows that the Fe-O bond cleavage in the intermediate may be the chiral discrimination step of the sulfoxidation.
已发现肌红蛋白的H64D/V68A和H64D/V68S突变体能够以高对映选择性和反应活性氧化苯甲硫醚。这些突变体还能够对α-甲基苄胺进行对映选择性结合,α-甲基苄胺模拟了预期的亚砜化中间体。对胺结合的动力学研究表明,中间体中的Fe-O键断裂可能是亚砜化的手性识别步骤。