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

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...

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Vydáno v:	Journal of the American Chemical Society Ročník 139; číslo 41; s. 14638
Hlavní autoři:	Gil, Agnieszka A, Laptenok, Sergey P, Iuliano, James N, Lukacs, Andras, Verma, Anil, Hall, Christopher R, Yoon, Grace E, Brust, Richard, Greetham, Gregory M, Towrie, Michael, French, Jarrod B, Meech, Stephen R, Tonge, Peter J
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States 18.10.2017
Témata:	Bacterial Proteins - metabolism Bacterial Proteins - radiation effects Binding Sites Color Electron Transport Flavin-Adenine Dinucleotide - metabolism Flavoproteins - metabolism Flavoproteins - radiation effects Fluorine - metabolism Hydrogen Bonding Hydrogen-Ion Concentration Light Photoreceptors, Microbial - metabolism Photoreceptors, Microbial - radiation effects Protein Domains Protons Synechocystis - chemistry Tyrosine - metabolism
ISSN:	1520-5126, 1520-5126
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