| 초록 |
Hydroxylation through soluble methane monooxygenase (sMMO) has been studied extensively to understand the biological conversion from methane to methanol in ambient conditions, although more detailed mechanisms of this biocatalyst are yet undiscovered. In this study, sMMO components, including the hydroxylase (MMOH), regulatory (MMOB), and reductase (MMOR), were expressed and purified from a type II methanotroph, Methylosinus sporium strain 5 (M. sporium 5), to characterize its hydroxylation mechanism. The cell extract showed that MMOH, MMOB, and MMOR were expressed by M. sporium 5, and these enzymes were extracted with high purity. The enzyme activity confirmed that 2.0 mol equivalents of MMOB is necessary to achieve catalytic activities, and sMMO from M. sporium 5 oxidized a broad range of substrates, including alkanes, alkenes, halogens, and aromatics. |
