Temperature dependence of protein fluorescence in Rb. sphaeroides reaction centers frozen to 80 K in the dark or on the actinic light as the indicator of protein conformational dynamics
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  • 作者:P. P. Knox ; B. N. Korvatovsky ; P. M. Krasilnikov…
  • 刊名:Doklady Biochemistry and Biophysics
  • 出版年:2016
  • 出版时间:March 2016
  • 年:2016
  • 卷:467
  • 期:1
  • 页码:105-109
  • 全文大小:256 KB
  • 刊物类别:Biomedical and Life Sciences
  • 刊物主题:Life Sciences
    Biochemistry
    Biophysics and Biomedical Physics
    Russian Library of Science
  • 出版者:MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
  • ISSN:1608-3091
  • 卷排序:467
文摘
The differences in the average fluorescence lifetime (τav) of tryptophanyls in photosynthetic reaction center (RC) of the purple bacteria Rb. sphaeroides frozen to 80 K in the dark or on the actinic light was found. This difference disappeared during subsequent heating at the temperatures above 250 K. The computer-based calculation of vibration spectra of the tryptophan molecule was performed. As a result, the normal vibrational modes associated with deformational vibrations of the aromatic ring of the tryptophan molecule were found. These deformational vibrations may be active during the nonradiative transition of the molecule from the excited to the ground state. We assume that the differences in τav may be associated with the change in the activity of these vibration modes due to local variations in the microenvironment of tryptophanyls during the light activation.Original Russian Text © P.P. Knox, B.N. Korvatovsky, P.M. Krasilnikov, V.Z. Paschenko, N.H. Seifullina, N.P. Grishanova, A.B. Rubin, 2016, published in Doklady Akademii Nauk, 2016, Vol. 467, No. 3, pp. 350–354.
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