Structure and Photoreaction of Photoactive Yellow Protein

Imamoto, Yasushi; Harigai, Miki; Shimizu, Nobutaka; Kamikubo, Hironari; Yamazaki, Yoichi; Kataoka, Mikio

추천

검색

자료유형: 학술저널

저자정보: Imamoto, Yasushi (Graduate School of Materials Science, Nara Institute of Science and Technology) Harigai, Miki (Graduate School of Materials Science, Nara Institute of Science and Technology) Shimizu, Nobutaka (Graduate School of Materials Science, Nara Institute of Science and Technology) Kamikubo, Hironari (Graduate School of Materials Science, Nara Institute of Science and Technology) Yamazaki, Yoichi (Graduate School of Materials Science, Nara Institute of Science and Technology) Kataoka, Mikio (Graduate School of Materials Science, Nara Institute of Science and Technology)

저널정보: 한국광과학회 Journal of photoscience : an international journal officail organ of the korean society of photoscience Journal of photoscience : an international journal officail organ of the korean society of photoscience 제9권 제2호

발행연도: 2002.1

수록면: 126 - 129 (4page)

이용수

📌

연구주제

📖

연구배경

🔬

연구방법

🏆

연구결과

초록· 키워드

오류제보하기

The chromophore/protein interactions in the photocycle intermediates of photoactive yel- low protein (PYP) were probed by site-directed mutagenesis. The absorption spectra of L- intermediates produced from E46Q, T50V, and R52Q mutants were calculated using the absorption spectra of dark states and difference absorption spectra between L-intermediates and dark states, and compared with that of PYP$\_$L/. The absorption spectrum of R52Q$\_$L/ agreed with that of PYP$\_$L/, but those of E46Q$\_$L/ and T50V$\_$L/ were red-shifted. The effect of these mutations on the absorption spectrum for L-intermediate was comparable to that for the dark state, suggesting that the interaction around the phe-nolic oxygen of the chromophore is conserved in PYP$\_$L/ unlike the crystal structure. On the other hand, we have reported that the absorption spectra of Y 42F$\_$M/, T50V $\_$M/, and R52Q$\_$M/ agreed with that of PYP$\_$M/, but that of E46Q$\_$M/ was red-shifted, suggesting that the hydrogen bond of the chromophore with Glu46 is conserved but that with Tyr42 is broken in PYP$\_$M/. These results suggest that the chromophore inter-acts with Glu46 throughout the photocycle, but never directly interacts with Arg52. This model con- flicts with some of the structural model of PYP intermediates proposed based on the high-resolution X -ray crystallography.

#X-ray crystallography #spectroscopy #photocycle #protein structure #photoreceptor

참고문헌 (0)

참고문헌 신청

참고문헌이 DBpia에서 서비스 중이라면, [참고문헌 신청]을 통해 등록해보세요

함께 읽어보면 좋을 논문

논문 유사도에 따라 DBpia 가 추천하는 논문입니다. 함께 보면 좋을 연관 논문을 확인해보세요!