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09월 10일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능
제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내
Reductase components and its electron transfer through
2019년 8월 28일 10시 15분 44초
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10월 17일 (목요일) 11:00~12:30
, Heeseon Yoo
, Seung Jae Lee
Department of Chemistry and Institute for Molecular Biology and Genetics, Chonbuk National University, Korea
The reduced diferrous state (Fe
) can in turn activate O
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,
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
, and it was purified to evaluate its catalytic activities using diverse substrates. MMOB and MMOR were also expressed in
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
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.
activity measurements demonstrated that alkanes, halogens, benzene, and toluene are oxidized through sMMO, and 2 mol equivalents of MMOB showed optimal activity.
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