Journal
FEBS LETTERS
Volume 581, Issue 28, Pages 5425-5429Publisher
WILEY
DOI: 10.1016/j.febslet.2007.10.043
Keywords
phytochrome; biliverdin; photoreceptor
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The bacteriophytochrome Agp1 was reconstituted with a locked 5Zs-biliverdin in which the C-4=C-5 and C-5-C-6 bonds of the methine bridge between rings A and B are fixed in the Z and syn configuration/conformation, respectively. In Agp1-5Zs the photoconversion proceeds via the Lumi-R intermediate to Meta-R-A, but the following millisecond-transition to Meta-R-C is blocked. Consistently, no transient proton release was detected. The photoconversion of Agp1-5Zs is apparently arrested in a Meta-R-A-like intermediate, since the subsequent syn to anti rotation around the C-5-C-6 bond is prevented by the lock. The Meta-R-A-like photoproduct was characterized by its distinctive CD spectrum suggesting a reorientation of ring D. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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