Orange carotenoid protein

[5] At the same time the protein was shown to be an effective quencher of singlet oxygen and was suggested to be involved in photoprotection, or carotenoid transport.

[6][7][8] In 2000, it was demonstrated that cyanobacteria could perform photoprotective fluorescence quenching independent of lipid phase transitions, differential transmembrane pH, and inhibitors.

[12] Photoactivation is accompanied by a pronounced color change, from orange to red, which had been previously observed by Kerfeld et al in the initial structural studies.

[7][8][5] In 2015 a combination of biophysical methods by researchers in Berkeley showed that the visible color change is the consequence of a 12Å translocation of the carotenoid.

[16] OCP is found in a majority of cyanobacterial genomes,[1][17] with remarkable conservation of its amino acid sequence, implying evolutionary constraints to preserve an important function.

[18] Under nutrient stress conditions, which are expected to be norm in marine environments, photoprotective mechanisms such as OCP become important even at lower irradiances.

[12][15] As evidenced by a decreased fluorescence, OCP in its red form is capable of dissipating absorbed light energy from the phycobilisome antenna complex.

[21][23][24] The temperature dependence of the rate of fluorescence quenching is similar to that of soluble protein folding,[25] supporting the hypothesis that OCPO slightly unfolds when it converts to OCPR.

In 2013 Kerfeld and co-workers showed that the NTD is the effector (quencher) domain of the protein while the CTD plays a regulatory role.

The activated OCPR form binds to allophycocyanin in the core of the phycobilisome and initiates the OCP-dependent photoprotective quenching mechanism.

Because of its high efficiency of fluorescence quenching, coupled to its low quantum yield of photoactivation by specific wavelengths of light, OCP has ideal properties as a photoswitch and has been proposed as a novel system for developing optogenetics technologies [1] and may have other applications in optofluidics and biophotonics.

Absorption spectrum of OCP in the inactive orange form vs the photoactivated red form
Ribbon view of the orange carotenoid protein molecular structure from Arthrospira maxima ( PDB code 1M98 ).