The Orange Carotenoid Protein (OCP) is a photoactive water soluble protein that is crucial for photoprotection in cyanobacteria. When activated by blue-green light, it triggers quenching of phycobilisome fluorescence and regulates energy flow from the phycobilisome to the reaction center. The OCP contains a single pigment, the carotenoid 3'-hydroxyechinenone (hECN). Binding to the OCP causes a conformational change in hECN leading to an extension of its effective conjugation length. We have determined the S(1) energy of hECN in organic solvent and compared it with the S(1) energy of hECN bound to the OCP. In methanol and n-hexane, hECN has an S(1) energy of 14,300cm(-1), slightly higher than carotenoids with shorter conjugation lengths such as zeaxanthin or β-carotene; this is consistent with the proposal that the presence of the conjugated carbonyl group in hECN increases its S(1) energy. The S(1) energy of hECN in organic solvent is independent of solvent polarity. Upon binding to the OCP, the S(1) energy of hECN is further increased to 14,700cm(-1), underscoring the importance of protein binding which twists the conjugated carbonyl group into s-trans conformation and enhances the effect of the carbonyl group. Activated OCP, however, has an S(1) energy of 14,000cm(-1), indicating that significant changes in the vicinity of the conjugated carbonyl group occur upon activation.

University of South Bohemia České Budějovice Czech Republic

Citace poskytuje Crossref.org

Structures of a phycobilisome in light-harvesting and photoprotected states

Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein

Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix

Ultrafast spectroscopy tracks carotenoid configurations in the orange and red carotenoid proteins from cyanobacteria