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  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Detergent-dependent oligomerization and coupling of spectral shift with spin state equilibrium in rice allene oxide synthase-1

등록일
2014년 8월 28일 16시 17분 05초
접수번호
1211
발표코드
BIO.P-643 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 15일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
YOEUNSEREYVATH, 한옥수1,*
전남대학교 생명공학과, Cambodia
1전남대학교 분자생명공학과, Korea

Allene oxide synthase (AOS) is a member of the cytochrome P450 subfamily 74 and converts fatty acid hydroperoxides into unstable fatty acid epoxides, which can be metabolized to 12-oxophytodienoic acid and subsequently undergoes reduction and β-oxidation to yield JA. In this study, biochemical and spectroscopic properties of rice allene oxide synthase-1 were characterized. OsAOS1 without any putative chloroplast targeting sequence was localized in chloroplast and showed steterospecific conversion of 9 and 13 di(tri)enoic hydrperoxy fatty acids. Oligomeric state of OsAOS1 was confirmed by cross-linking experiments. UV-Visible spectral analysis of native OsAOS1 revealed a Soret maximum at 393 nm, which shifted to 424 upon binding of OsAOS1 to imidazole, which were correlated with inhibition of OsAOS1 activity. F92L point mutation enhanced HPL activity and spectral shifts of Soret maximum were observed with P430A and F92L/P430A mutants. We analyzed spin state population of OsAOS1 by EPR and compared with the spectral shift induced by imidazole. Our results suggest that detergent-dependent oligomeric state of OsAOS1 is an important factor for the regulation of its catalytic efficiency and provide evidences that the imidazole ligand binds to iron(III) as the sixth ligand (distal position) and drives the spin state equilibrium toward low spin state of iron(III) in OsAOS1.


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