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  • 02월 20일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제113회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Interaction of NO with Heme Proteins Probed by Femtosecond IR Spectroscopy

2014년 2월 28일 09시 34분 32초
PHYS2-1 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 13시 : 25분
물리화학 - Physical Chemistry at the Nanoscale
저자 및
부산대학교 화학과, Korea
Nitric oxide (NO), a key cellular signaling molecule in many biological systems, regulates and mediates diverse processes. NO-bound heme adducts are observed frequently in various biological processes that involve NO signaling. Unlike CO and O2 that bind only ferrous heme, NO can bind to both ferrous and ferric hemes, which contributes to a number of biological functions of NO in vivo. The rebinding dynamics of NO to various heme proteins after the photolysis of NO-bound adducts has been probed to reveal the NO-binding mechanism and to elucidate how the binding of NO to heme proteins is controlled by the structure and dynamics of proteins. The geminate rebinding (GR) of NO to ferrous-heme proteins is extremely efficient and proceeds on picosecond time scales, which has been attributed to the high reactivity of NO toward the Fe(II) of the heme. Nitrosylated ferric heme is autoreduced readily to the more stable Fe(II)?NO adduct but it is stabilized in NO-carrier heme proteins where maintaining the Fe(III) oxidation state is crucial for efficient NO delivery. Density functional theory calculations have shown that a NO-bound ferric model heme has a low-spin Fe(III)?NO(radical) state that might be critical for efficient NO transport by NO-carrier heme proteins. The elusive R state was investigated after photoexcitation of NO-bound ferric heme proteins using femtosecond time-resolved vibrational spectroscopy. Experimental findings will be presented in the conference.