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

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Rebinding dynamics of CO with Cytoglobin in aqueous solution using ultrafast vibrational spectroscopy

2014년 8월 28일 15시 43분 27초
PHYS.P-438 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 15일 (수요일) 16:00~19:00
저자 및
김주영, 임만호*, 이태곤
부산대학교 화학과, Korea
Recently, Cytoglobin, a heme-containing protein, was found in vertebrates. It is found in a wide range of mammalian tissues and is also available to bind with external ligands. Unlike myoglobin Fe in heme plane of Cgb is six coordinated with distal and proximal histidine. In this study, We measured the rebinding dynamics of the CO complex of Cytoglobin in aqueous solution using femtosecond and nanosecond vibrational spectroscopy. The stretching mode of CO bound to the protein shows three stretching bands at 1924 cm-1(A0), 1899 cm-1(A1) and 1884 cm-1(A3) . Ligand binding to Cgb is a multiphasic process with fast geminate rebinding taking place on the nanosecond timescales and slower bimolecular rebinding occurring on microsecond timescales. The geminate rebinding of CO to Cgb is about 40%, more efficient than that of myoglobin(4%), ligand binding protein has primary heme pocket. The fast geminate rebinding of CO to Cgb was from the distal histidine imidazole oriented out of the heme pocket in a similar way as observed for the distal histidine in Mb at low pH, open conformations(A0). It suggests that according to conformations of protein affects rebinding kinetics of photolized CO.