Locked 5Zs‐biliverdin blocks the Meta‐RA to Meta‐RC transition in the functional cycle of bacteriophytochrome Agp1

The bacteriophytochrome Agp1 was reconstituted with a locked 5Zs‐biliverdin in which the C4 C5 and C5–C6 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...

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Bibliographic Details
Published in:FEBS letters 2007-11, Vol.581 (28), p.5425-5429
Main Authors: Seibeck, Sven, Borucki, Berthold, Otto, Harald, Inomata, Katsuhiko, Khawn, Htoi, Kinoshita, Hideki, Michael, Norbert, Lamparter, Tilman, Heyn, Maarten P.
Format: Article
Language:English
Subjects:
18-ethyl biliverdin
18EtBV
Amino Acid Transport Systems, Neutral - metabolism
Bacterial Proteins - metabolism
biliverdin
Biliverdine - chemistry
Biliverdine - pharmacology
Circular Dichroism
far-red-absorbing form of phytochrome
Hydrogen-Ion Concentration
Kinetics
Light
Molecular Structure
Pfr
Photochemistry
Photoreceptor
Phytochrome
Phytochrome - chemistry
Phytochrome - metabolism
Protons
red-absorbing form of phytochrome
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Summary:The bacteriophytochrome Agp1 was reconstituted with a locked 5Zs‐biliverdin in which the C4 C5 and C5–C6 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‐RA, but the following millisecond‐transition to Meta‐RC is blocked. Consistently, no transient proton release was detected. The photoconversion of Agp1‐5Zs is apparently arrested in a Meta‐RA‐like intermediate, since the subsequent syn to anti rotation around the C5–C6 bond is prevented by the lock. The Meta‐RA‐like photoproduct was characterized by its distinctive CD spectrum suggesting a reorientation of ring D.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.10.043