@npigni
A favorable path to domain separation in the orange carotenoid protein (Protein Sci. 2022, 31, 4, 850–863)
A favorable path to domain separation in the orange carotenoid protein (Protein Sci. 2022, 31, 4, 850–863)
Spectral Signatures of Canthaxanthin Translocation in the Orange Carotenoid Protein (J. Phys. Chem. B 2020, 124, 50, 11387–11395)
Spectral Signatures of Canthaxanthin Translocation in the Orange Carotenoid Protein (J. Phys. Chem. B 2020, 124, 50, 11387–11395)
The orange carotenoid protein (OCP) is involved in the photoprotective processes in cyanobacteria via nonphotochemical quenching. Triggered by blue-green light absorption, the carotenoid chromophore undergoes translocation, displacing around 12 Å from the C-terminal domain (CTD) to the N-terminal domain (NTD). The detailed molecular rearrangements that occur within the carotenoid and the protein during this process remain largely elusive. By using a combination of molecular dynamics, well-tempered metadynamics, and hybrid quantum mechanical/molecular mechanical (QM/MM) calculations, we were able to mimic the translocation of the carotenoid from the inactive OCPO and obtain metastable red-shifted states in the photoactivation mechanism, replicating the λmax values of reference experimental spectra. In addition, our simulations give insight into the structure of the red-shifted form of the inactive state of OCP.
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