Photoactive Yellow Protein Chromophore Photoisomerizes around a Single Bond if the Double Bond Is Locked.

ABSTRACT: Photoactivation in the Photoactive Yellow Protein, a bacterial blue-light photoreceptor, proceeds via photoisomerization of the double C═C bond in the covalently attached chromophore. Quantum chemistry calculations, however, have suggested that in addition to double-bond photoisomerization, the isolated chromophore and many of its analogues can isomerize around a single C-C bond as well. Whereas double-bond photoisomerization has been observed with X-ray crystallography, experimental evidence of single-bond photoisomerization is currently lacking. Therefore, we have synthesized a chromophore analogue, in which the formal double bond is covalently locked in a cyclopentenone ring, and carried out transient absorption spectroscopy experiments in combination with nonadiabatic molecular dynamic

SUBMITTER: Mustalahti S 

PROVIDER: S-EPMC7145348 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature