Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.

ABSTRACT: The flavin chromophore in blue-light-using FAD (BLUF) photoreceptors is surrounded by a hydrogen bond network that senses and responds to changes in the electronic structure of the flavin on the ultrafast time scale. The hydrogen bond network includes a strictly conserved Tyr residue, and previously we explored the role of this residue, Y21, in the photoactivation mechanism of the BLUF protein AppA_BLUF by the introduction of fluorotyrosine (F-Tyr) analogues that modulated the pK_a and reduction potential of Y21 by 3.5 pH units and 200 mV, respectively. Although little impact on the forward (dark- to light-adapted form) photoreaction was observed, the change in Y21 pK_a led to a 4000-fold increase in the rate of dark-state recovery. In the present work we have

SUBMITTER: Gil AA 

PROVIDER: S-EPMC5647244 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature