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학술발표회초록보기

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제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 MMOD-induced structural changes of hydroxylase in soluble methane monooxygenase

등록일
2019년 8월 29일 12시 57분 11초
접수번호
1789
발표코드
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발표시간
목 09시 : 45분
발표형식
구두발표
발표분야
Life Chemistry - Oral Presentations by Young Life Chemists
저자 및
공동저자
Hanseong Kim, Minseok Kwak, Seung Jae Lee1, Uhn-Soo Cho2,*
Department of Chemistry, Pukyong National University, Korea
1Department of Chemistry, Chonbuk National University, Korea
2Department of Biological Chemistry, University of Michigan, U.S.A., United States
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승인 1건

Soluble methane monooxygenase in methanotrophs converts methane to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay of its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor of MMOH; however, its inhibitory mechanism remains unknown. Herein, we report the crystal structure of the MMOH–MMOD complex from Methylosinus sporium strain 5 (2.6 Å). Its structure illustrates that MMOD associates with the canyon region of MMOH where MMOB binds. Although MMOD and MMOB recognize the same binding site, each binding component triggers different conformational changes toward MMOH, which then respectively lead to the inhibition and activation of MMOH. Particularly, MMOD binding perturbs the di-iron geometry by inducing two major MMOH conformational changes, i.e., MMOH β-subunit disorganization and subsequent His147 dissociate with on Fe1 coordination. Furthermore, 1,6-hexanediol, a mimic of the products of sMMO, reveals the substrate access route.


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