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

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0014-5793 (Print) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
    • Publication Information:
      Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
      Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
    • Subject Terms:
      Amino Acid Transport Systems, Neutral/*metabolism ; Bacterial Proteins/*metabolism ; Biliverdine/*pharmacology ; Phytochrome/*metabolism; Biliverdine/chemistry ; Circular Dichroism ; Hydrogen-Ion Concentration ; Kinetics ; Light ; Molecular Structure ; Photochemistry ; Phytochrome/chemistry ; Protons
    • Abstract:
      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.
    • Accession Number:
      0 (Amino Acid Transport Systems, Neutral)
      0 (Bacterial Proteins)
      0 (Protons)
      11121-56-5 (Phytochrome)
      O9MIA842K9 (Biliverdine)
    • Publication Date:
      Date Created: 20071103 Date Completed: 20080204 Latest Revision: 20131121
    • Publication Date:
      20250114
    • Accession Number:
      10.1016/j.febslet.2007.10.043
    • Accession Number:
      17976380