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자료유형
학술저널
저자정보
Sonoyama, Masashi (Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology) Mitaku, Shigeki (Department of Biotechnology and Life Science, Tokyo University of Agriculture 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
299 - 301 (3page)

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Recent denaturation experiments of bacteriorhodopsin (bR) in the dark and under illumination at high temperatures revealed that irreversible thermal bleaching occurs above ~ 70°C and the preceding reversible structural changes in the dark above 60°C are closely related to irreversible photobleaching observed in the same temperature range (Yokoyama et al. (2002). J Biochem. 131,785). In this study, structural properties of bacteriorhodopsin (bR) at high temperatures were extensively probed by hydroxylamine reactivity with the Schiff base in the dark and hydrogen-deuterium (H-D) exchange in the peptide groups. In the Arrhenius plot from kinetics measurements of the hydroxylamine reaction, a good linear relationship between the reaction time constant and the inverse of the absolute temperature was observed below 60°C, while significant increase started above 60°C, suggesting that remarkable increase in water accessibility of the Schiff base in the temperature region. FT-IR spectroscopic studies on the H-D exchange suggested increase in the deuterium exchanges rate of the peptide hydrogen in the same temperature region.

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