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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Bibliographic Details
Published in:	Journal of the American Chemical Society Vol. 139; no. 41; p. 14638
Main Authors:	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
Format:	Journal Article
Language:	English
Published:	United States 18.10.2017
Subjects:	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
Online Access:	Get more information
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