Neutron crystallography of photoactive yellow protein reveals unusual protonation state of Arg52 in the crystal
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-09718-9.pdf
Reference40 articles.
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2. Xiao, Y., Hutson, M. S., Belenky, M., Herzfeld, J. & Braiman, M. S. Role of arginine-82 in fast proton release during the bacteriorhodopsin photocycle: A time-resolved FT-IR study of purple membranes containing 15N-labeled arginine. Biochemistry 43, 12809–12818 (2004).
3. Yamaguchi, S. et al. Low-barrier hydrogen bond in photoactive yellow protein. Proc. Natl. Acad. Sci. USA 106, 440–444 (2009).
4. Meyer, T. E. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim. Biophys. Acta 806, 175–183 (1985).
5. Sprenger, W. W., Hoff, W. D., Armitage, J. P. & Hellingwerf, K. J. The Eubacterium Ectothiorhodospira-halophila Is negatively phototactic, with a wavelength dependence that fits the absorption-spectrum of the photoactive yellow protein. J. Bacteriol. 175, 3096–3104 (1993).
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