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  The Central Role of Gln63 for the Hydrogen Bonding Network and UV-Visible Spectrum of the AppA BLUF Domain

Hsiao, Y.-W., Götze, J., & Thiel, W. (2012). The Central Role of Gln63 for the Hydrogen Bonding Network and UV-Visible Spectrum of the AppA BLUF Domain. The Journal of Physical Chemistry B, 116(28), 8064-8073. doi:10.1021/jp3028758.

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Hsiao, Y.-W.1, Author           
Götze, Jan1, Author           
Thiel, Walter1, Author           
Affiliations:
1Research Department Thiel, Max-Planck-Institut für Kohlenforschung, Max Planck Society, ou_1445590              

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 Abstract: In blue-light sensing using flavin (BLUF) domains, the side-chain orientation of key residues close to the flavin chromophore is still under debate. We report quantum refinements of the wild-type AppA BLUF protein from Rhodobacter sphaeroides starting from two published X-ray structures (1YRX and 2IYG) with different arrangements of the residues around the chromophore. Quantum refinement uses the same experimental X-ray raw data as conventional refinement, but includes data from quantum mechanics/molecular mechanics (QM/MM) calculations as restraints, which is expected to be more reliable than the normally employed MM data. In addition to quantum refinement, pure QM/MM geometry optimizations are performed for the 1YRX and 2IYG structures and for five models derived therefrom. Vertical excitation energies are computed at the QM(DFT/MRCI)/MM level to assess the resulting structures. The experimental absorption maximum of the dark state of wild-type AppA is well reproduced for structures that contain the Gln63 residue in 1YRX-type orientation. The computed excitation energies are red-shifted for structures with a flipped Gln63 residue in 2IYG-type orientation. The calculated 1YRX- and 2IYG-type hydrogen-bonding networks are discussed in detail, particularly with regard to the orientation of the chromophore and the Gln63, Trp104, and Met106 residues.

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 Dates: 2012-07-19
 Publication Status: Issued
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 Identifiers: DOI: 10.1021/jp3028758
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Title: The Journal of Physical Chemistry B
Source Genre: Journal
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Pages: - Volume / Issue: 116 (28) Sequence Number: - Start / End Page: 8064 - 8073 Identifier: ISSN: 1520-6106
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000293370_1
DOI: 10.1021/jp3028758