| 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 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. Optimal activities were observed at pH 7.5 in most substrates, possibly because of the electron transfer environment in MMOR, and this was explained by the optical spectra from FAD-containing domains. |
