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제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Reductase components and its electron transfer through

2019년 8월 28일 10시 15분 44초
INOR.P-101 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 17일 (목요일) 11:00~12:30
Inorganic Chemistry
저자 및
Chungwoon Yoon, Heeseon Yoo, Seung Jae Lee*
Department of Chemistry and Institute for Molecular Biology and Genetics, Chonbuk National University, Korea
The reduced diferrous state (FeIIFeII) can in turn activate O2 and initiate a catalytic cycle. MMOB does not have any metal ions and coenzymes; however, this regulatory enzyme acts on the pore region near to the diiron active sites, containing the residues Thr213, Asn214, and Glu240, which are considered key regulators for the electron and/or proton transfer. Catalytic activities are improved in the presence of MMOB and MMOH–MMOB complex, indicating that two MMOB molecules can bind to the hydroxylase component at the diiron active site, regulating methane hydroxylation. The structural information between MMOH and MMOR is required to discover the electron transfer pathway that is crucial for turnover number. Recent studies have proposed that the ferredoxin domain of MMOR shares the binding site with MMOB located in the canyon region of MMOH for electron transfer. In this study, M. sporium 5 was cultured in a tightly regulated NMS media by supplying methane and air to understand its growth and the expression levels of multi-component enzymes. MMOH was found to be highly expressed in M. sporium 5, and it was purified to evaluate its catalytic activities using diverse substrates. MMOB and MMOR were also expressed in E. coli via constructed plasmids to obtain highly purified enzymes. The successfully expressed and purified enzymes were utilized to measure specific enzyme activities (SEA), and these results showed that M. sporium 5 exhibits optimal activity at pH 7.5. The electron transfer environment of MMOR is crucial for the activity of sMMO, and different acidities may change the electron transfer environment. In vitro activity measurements demonstrated that alkanes, halogens, benzene, and toluene are oxidized through sMMO, and 2 mol equivalents of MMOB showed optimal activity.