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  Quantum chemistry calculations provide support to the mechanism of the light-induced structural changes in the flavin-binding photoreceptor proteins

Khrenova, M. G., Nemukhin, A. V., Grigorenko, B. L., Krylov, A. I., & Domratcheva, T. (2010). Quantum chemistry calculations provide support to the mechanism of the light-induced structural changes in the flavin-binding photoreceptor proteins. Journal of Chemical Theory and Computation, 6(8), 2293-2302. doi:10.1021/ct100179p.

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Genre: Journal Article
Alternative Title : Quantum Chemistry Calculations Provide Support to the Mechanism of the Light−Induced Structural Changes in the Flavin−Binding Photoreceptor Proteins

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JChemTheoryComput_6_2010_2293.pdf (Any fulltext), 386KB
 
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Khrenova, M. G., Author
Nemukhin, Alexander V., Author
Grigorenko, Bella L., Author
Krylov, A. I., Author
Domratcheva, Tatiana1, Author              
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: The proposed mechanisms of photoinduced reactions in the blue light using flavin chromophore photoreceptor proteins are primarily based on the results of X-ray crystallography and spectroscopy studies. Of particular value are the observed band shifts in optical and vibrational spectra upon formation of the signaling (light-induced) state. However, the same set of experimental data has given rise to contradictory interpretations suggesting different structures of the dark and signaling states. To verify the specific mechanism of light-induced changes involving the rotation/tautomerization transformations with the conserved Gln residue near the flavin chromophore, we performed accurate quantum chemical calculations of the equilibrium structures, vibrational and absorption bands of the model systems mimicking the BLUF domain of flavoprotein AppA. Geometry optimization and calculations of vibrational frequencies were carried out with the QM(B3LYP/cc-pVDZ)/MM(AMBER) approach starting from the representative molecular dynamics (MD) snapshots. The MD simulations were initiated from the available crystal structures of the AppA protein. Calculations of the vertical excitation energies were performed with the scaled opposite spin configuration interaction with single substitutions SOS-CIS(D) method that enables efficient treatment of excited states in large molecular systems. The computed molecular structures as well as the spectral shifts (the red shift by 12÷16 nm in absorption and the downshift by 25 cm−1 for the C4═O flavin vibrational mode) are in excellent agreement with the experimental results, lending a strong support to the mechanism proposed by Domratcheva et al. (Biophys. J. 2008, 94, 3872).

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Language(s): eng - English
 Dates: 2010-04-052010-07-012010-08-10
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664553
DOI: 10.1021/ct100179p
URI: http://pubs.acs.org/doi/abs/10.1021/ct100179p
Other: 7612
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Title: Journal of Chemical Theory and Computation
  Other : J. Chem. Theory Comput.
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 6 (8) Sequence Number: - Start / End Page: 2293 - 2302 Identifier: Other: 1549-9618
CoNE: https://pure.mpg.de/cone/journals/resource/111088195283832