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제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Diiron monooxygenase and substrate hydroxylation through multicomponent enzymes

등록일
2019년 8월 28일 13시 40분 44초
접수번호
1672
발표코드
INOR.P-103 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 17일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
Inorganic Chemistry
저자 및
공동저자
Jaewoong Park, Heeseon Yoo, Seung Jae Lee*
Department of Chemistry and Institute for Molecular Biology and Genetics, Chonbuk National University, Korea
Methane (CH4) is considered as one of the most important greenhouse gases owing to its 20-fold higher heat capacity compared with that of carbon dioxide (CO2). Preliminary studies have aimed to elucidate the mechanisms of soluble methane monooxygenase (sMMO) involved in this extremely stable C–H activation (104.9 kcal/mol) through intermediate studies, advanced spectroscopies, and structural researches, mostly in Methylosinus trichosporium OB3b and Methylococcus capsulatus Bath, although mechanistic studies are still required. To better understand the mechanism of sMMO, we successfully expressed and purified essential components, including MMOH, MMOB, and reductase (MMOR) components from Methylosinus sporium 5. MMOH from M. sporium 5 was successfully expressed and purified from the native bacteria, and MMOB and MMOR were expressed and purified from E. coli using recombinant plasmids. We report the first enzymatic study of highly purified essential components, including MMOH, MMOB, and MMOR. Each component was successfully characterized, and specific enzyme activities were comparable with those of other sMMOs with non-heme diiron active sites. Specific enzyme activity showed that two mole equivalents of MMOB/MMOH demonstrate maximal activity in the presence of substrates and one mole equivalent of MMOR/MMOH is sufficient for this activity. Most substrates showed maximal specific enzyme activities at pH 7.5, and these were confirmed by spectroscopic studies on MMOR and the FAD-domain of MMOR by the subtle changes in the interaction between flavin and MMOR.

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