Abstract
Light-dependent changes around the protonated Schiff base of bacteriorhodopsin were studied by low temperature FTIR spectroscopy on intermediates K, L, M and N. A special effort was done for the recording of the spectrum of N. Upon formation of L, a strong hydrogen bonding occurs between the Schiff base and the aspartic acid residues. It causes the twisting of the chromophore. Such a twisting is lost during the stage of M and the strong interaction with the aspartic acid residues reforms upon formation of N.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
G. Varo, J. K. Lanyi: Biochemistry 29, 2241 (1990).
S. Y. Liu: Biophys. J. 57, 943 (1990).
L. A. Drachev, A. D. Kaulen, V. P. Skulachev, V. V. Zorina: FEBS Lett. 226, 139 (1987).
A. Maeda, T. Ogura, T. Kitagawa: Biochemistry 25, 2793 (1986).
T. Kouyama, A. -N. Kouyama, A. Ikegami, M. K. Mathew, W. Stoeckenius: Biochemistry 27, 5855 (1988).
J.-M. Pfefferle, A. Maeda, J. Sasaki, T. Yoshizawa: Biochemistry in press (1991).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1992 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Maeda, A., Pfefferlé, JM., Sasaki, J., Shichida, Y., Yoshizawa, T. (1992). Low Temperature FTIR Studies on the Photointermediates L, M, and N of Bacteriorhodopsin. In: Takahashi, H. (eds) Time-Resolved Vibrational Spectroscopy V. Springer Proceedings in Physics, vol 68. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-84771-4_20
Download citation
DOI: https://doi.org/10.1007/978-3-642-84771-4_20
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-84773-8
Online ISBN: 978-3-642-84771-4
eBook Packages: Springer Book Archive