Jump to main content
Jump to site search

Issue 32, 2011
Previous Article Next Article

Why BLUF photoreceptors with roseoflavin cofactors lose their biological functionality

Author affiliations

Abstract

The photophysics of roseoflavin in three different environments is investigated by using ab initio and quantum mechanics/molecular mechanics methods. Intramolecular charge transfer is shown to be responsible for the quenching of the fluorescence in the gas phase, and in the water environment. However, for the roseoflavin incorporated into the blue light using flavin (BLUF) protein environment (substituting the native flavin) no such deactivation is found. The conical intersection between the locally excited state of the chromophore and the charge transfer state involving the tyrosine residue, which in the native BLUF domain is responsible for initiating the photocycle, is missing for the roseoflavin substituted protein. This explains the experimental observations of the lack of any photocycle, and the loss of the biological function of the BLUF photoreceptor reported earlier.

Graphical abstract: Why BLUF photoreceptors with roseoflavin cofactors lose their biological functionality

Back to tab navigation

Supplementary files

Publication details

The article was received on 02 May 2011, accepted on 16 Jun 2011 and first published on 12 Jul 2011


Article type: Paper
DOI: 10.1039/C1CP21386E
Citation: Phys. Chem. Chem. Phys., 2011,13, 14775-14783
  •   Request permissions

    Why BLUF photoreceptors with roseoflavin cofactors lose their biological functionality

    T. Merz, K. Sadeghian and M. Schütz, Phys. Chem. Chem. Phys., 2011, 13, 14775
    DOI: 10.1039/C1CP21386E

Search articles by author

Spotlight

Advertisements