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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biomolekulare Mechanismen     Display Documents



ID: 420164.0, MPI für medizinische Forschung / Abteilung Biomolekulare Mechanismen
Molecular models predict light−induced glutamine tautomerization in BLUF photoreceptors
Translation of Title:Molecular models predict light−induced glutamine tautomerization in BLUF photoreceptors
Authors:Domratcheva, Tatiana; Grigorenko, Bella L.; Schlichting, Ilme; Nemukhin, Alexander V.
Language:English
Date of Publication (YYYY-MM-DD):2008-05-15
Title of Journal:Biophysical Journal
Journal Abbrev.:Biophys. J.
Volume:94
Issue / Number:10
Start Page:3872
End Page:3879
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The recently discovered photoreceptor proteins containing BLUF (sensor of blue light using FAD) domains mediate physiological responses to blue light in bacteria and euglenas. In BLUF domains, blue light activates the flavin chromophore yielding a signaling state characterized by a ˜ 10 nm red−shifted absorption. We developed molecular models for the dark and light states of the BLUF domain of the Rhodobacter sphaeroides AppA protein, which are based on the crystal structures and quantum−mechanical simulations. According to these models, photon absorption by the flavin results in a tautomerization and 180 degree rotation of the Gln side chain that interacts with the flavin cofactor. This chemical modification of the Gln residue induces alterations in the hydrogen bond network in the core of the photoreceptor domain, which were observed in numerous spectroscopic experiments. The calculated electronic transition energies and vibrational frequencies of the proposed dark and light states are consistent with the optical and IR spectral changes observed during the photocycle. Light−induced isomerization of an amino acid residue instead of a chromophore represents a feature that has not been previously described in photoreceptors.
Last Change of the Resource (YYYY-MM-DD):--
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI f�r medizinische Forschung/Abteilung Biomolekulare Mechanismen
External Affiliations:M. V. Lomonosov
Moscow State University, Department of Chemistry, 1/3, Moscow, 119992, Russian Federation; N. M. Emanuel Institute of Biochemical
Physics, Russian Academy of Sciences, 4, Moscow, 119334, Russian Federation
Identifiers:LOCALID:7180
URI:http%3A%2F%2Fwww.biophysj.org%2Fcgi%2Freprint%2F94...
URI:http%3A%2F%2Fwww.biophysj.org%2Fcgi%2Fcontent%2Ffu...
URI:http%3A%2F%2Fwww.biophysj.org%2Fcgi%2Fcontent%2Fab...
DOI:10.1529%2Fbiophysj.107.124172
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