Journal
FEBS LETTERS
Volume 585, Issue 1, Pages 167-172Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.11.035
Keywords
LOV domain; Cryptochrome; Redox titration; Site-directed mutation; Reduced and oxidized FAD; Flavin semiquinone
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The redox-midpoint potential of the FAD chromophore in the BLUF domain of anti-transcriptional regulator AppA from Rhodobacter sphaeroides equals similar to-260 mV relative to the calomel electrode. Altering the structure of its chromophore-binding pocket through site-directed mutagenesis brings this midpoint potential closer to that of free flavin in aqueous solution. The redox-midpoint potential of this BLUF domain is intermediate between those of LOV domains and Cryptochromes, which may rationalize the primary photochemistry observed in these three flavin-containing photoreceptor families. These results also imply that LOV domains, among the flavin-containing photosensory receptors, are least sensitive to intracellular chemical reduction in the dark. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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