Publication: Effects of the disappearance of one charge on ultrafast fluorescence dynamics of the FMN binding protein
Issued Date
2010-05-13
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ISSN
15205207
15206106
15206106
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2-s2.0-77952200626
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Physical Chemistry B. Vol.114, No.18 (2010), 6175-6182
Suggested Citation
Haik Chosrowjan, Seiji Taniguchi, Noboru Mataga, Takeshi Nakanishi, Yoshihiro Haruyama, Shuta Sato, Masaya Kitamura, Fumio Tanaka Effects of the disappearance of one charge on ultrafast fluorescence dynamics of the FMN binding protein. Journal of Physical Chemistry B. Vol.114, No.18 (2010), 6175-6182. doi:10.1021/jp912137s Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/28942
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Title
Effects of the disappearance of one charge on ultrafast fluorescence dynamics of the FMN binding protein
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Abstract
Crystal structures of E13T (Glu13 was replaced by Thr13) and E13Q (Glu13 was replaced by Gln13) FMN binding proteins (FMN-bp) from Desulfovibrio vulgaris, strain Miyazaki F, were determined by the X-ray diffraction method. Geometrical factors related to photoinduced electron transfer from Trp32, Tyr35, and Trp106 to the excited isoalloxazine (Iso) were compared among the three forms of FMN-bp. The rate of ET is considered to be fastest from Trp32 to Iso* in FMN-bp and then from Tyr35 and Trp106. The distances between Iso and Trp32 did not change appreciably (0.705-0.712 nm) among WT, E13T, and E13Q FMN-bps, though the distances between Iso and Tyr35 or Trp106 became a little shorter by ca. 0.01 nm in both mutated FMN-bps. The distances between the residue at 13 and the ET donors or acceptor in the mutated proteins, however, changed markedly, compared to WT. Hydrogen bonding pairs and distances between Iso and surrounding amino acids were not modified when Glu13 was replaced by Thr13 or Gln13. Effects of elimination of ionic charge at Glu13 on the ultrafast fluorescence dynamics in E13T and E13Q were investigated comparing to WT, by means of a fluorescence up-conversion method. Fluorescence lifetimes were α1= 107 fs (α1= 0.86), α2= 475 fs (α2= 0.12), and α3= 30 ps (α3= 0.02) in E13T and α1= 134 fs (α1= 0.85), α2= 746 fs (α2= 0.12), and α3= 30 ps (α3= 0.03) in E13Q, which are compared to the reported lifetimes in WT, α1= 168 fs (α1= 0.95) and α2= 1.4 ps (α2= 0.05). Average lifetimes (αAV= α=12or3αiα.,i) were 0.75 ps in E13T, 1.10 ps in E13Q, and 0.23 ps in WT, which implies that αAVwas 3.3 times longer in E13T and 4.8 times longer in E13Q, compared to WT. The ultrafast fluorescence dynamics of WT did not change when solvent changed from H2O to D2O. Static ET rates (inverse of average lifetimes) were analyzed with static structures of the three systems of FMN-bp. Net electrostatic (ES) energies of Iso and Trp32, on which ET rates depend, were 0.0263 eV in WT, 0.322 eV in E13T, and 0.412 eV in E13Q. The calculated ET rates were in excellent agreement with the observed ones in all systems. © 2010 American Chemical Society.