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Accurate evaluation of the absorption maxima of retinal proteins based on a hybrid QM/MM method
Author(s) -
Matsuura Azuma,
Sato Hiroyuki,
Houjou Hirohiko,
Saito Shino,
Hayashi Tomohiko,
Sakurai Minoru
Publication year - 2006
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.20432
Subject(s) - maxima , retinal , absorption (acoustics) , chromophore , deprotonation , chemistry , protonation , qm/mm , maxima and minima , photochemistry , computational chemistry , optics , physics , molecular dynamics , organic chemistry , mathematics , art , ion , mathematical analysis , biochemistry , performance art , art history
Here we improved our hybrid QM/MM methodology (Houjou et al. J Phys Chem B 2001, 105, 867) for evaluating the absorption maxima of photoreceptor proteins. The renewed method was applied to evaluation of the absorption maxima of several retinal proteins and photoactive yellow protein. The calculated absorption maxima were in good agreement with the corresponding experimental data with a computational error of <10 nm. In addition, our calculations reproduced the experimental gas‐phase absorption maxima of model chromophores (protonated all‐trans retinal Schiff base and deprotonated thiophenyl‐ p ‐coumarate) with the same accuracy. It is expected that our methodology allows for definitive interpretation of the spectral tuning mechanism of retinal proteins. © 2006 Wiley Periodicals, Inc. J Comput Chem, 2006