藉由細胞色素 P450 BM-3 突變株調控含氟化合物進行氧化時的立體及位置選擇性

Abstract

To initiate the C-H bond oxidation of aliphatic compounds is a great challenge for synthetic chemists. The conventional synthetic methods and industrial processes are usually required with extremely high temperature and high pressure to carry out the corresponding events. However, some of the gram-negative bacteria, like methanotropic bacteria, Pseudomonas spp. and Bacillus megaterium can facilely convert the aliphatic fine chemicals to the corresponding alcohols or oxiranes at ambient temperature and pressure. To understand how the C-H bond get activated in these microorganisms have withdrew great interest. In this study, cytochrome P450 BM-3 A74G F87V L188Q (3mt protein) and its variant A328F (A74G F87V L188Q A328F) adapted with its oxidoreductase in E. coli BL21(DE3) was used to convert designed fluorinated C8 alkanes to the corresponding alcohols in whole cell catalytic manner. We aim to probe the hydrophobic pockets within the enzymes. With the products variants by comparison with the results emerged from n-octane derivatives, we would have better understanding how C-F bond behaved like C-H bond to control the orientation of the substrates for their controlled oxidation. The obtained results would lead with the great insights for developing facile bio-related catalysts. The corresponding chemicals conversion could be utilitized as facile building blocks for the applications of organic synthesis in green chemistry approach.