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제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Coupling of spectral shift with spin state equilibrium in the inhibition of rice allene oxide synthase-1 by imidazole

등록일
2014년 8월 28일 15시 51분 24초
접수번호
1152
발표코드
BIO.P-639 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 cytochrome P450 subfamily (CYP74) and plays an important role in octadecaoind pathway and defense signaling in plants. CYP74 enzymes are non-classical cytochrome P450 in which molecular oxygen and NADPH-dependent P450 reductase are not required for the catalytic turn over. Instead, CYP74 family enzymes use a hydroperoxide group both as the activated oxygen donor and as a source of reducing equivalents. AOS can utilize 13(S)-hydroperoxyoctadecadi(tri)enoic acid (13(S)-HPOD(T)E) or 9(S)-hydroperoxyoctadecadi(tri)enoic acid (9(S)-HPOD(T)E) as a substrate depending on the specificity, which is converted into the corresponding allene oxide, 12,13-epoxy-9,11-octadecadienoic acid (12,13-EOD(T)) or 9,10-epoxy-10,12,(15)-octadecadi(tri)enoic acid (9,10-EOD(T)). In this study, biochemical and spectroscopic properties of rice allene oxide synthase-1 were characterized. 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. we analyzed spin state population of OsAOS1 by EPR and compared with the spectral shift induced by imidazole. Our results 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. The possible dehydration mechanism of OsAOS1 is proposed.


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