To cope with the deleterious effects of excess illumination, photosynthetic organisms have developed photoprotective mechanisms that dissipate the absorbed excess energy as heat from the antenna system. In cyanobacteria, a crucial step in the process is the activation, by blue-green light, of a soluble protein, known as orange carotenoid protein (OCP), which binds the carotenoid 3′-hydroxyechinenone as its only pigment. While the spectroscopic properties of the inactive form of OCP have been described, the nature of the excited states in the active form still awaits elucidation. We applied transient absorption spectroscopy to the dark and the light activated forms of OCP to study and compare the excited state dynamics of both forms. We show that excitation of the photoactivated OCP leads to the population of new carotenoid excited states. One of these states populated shortly after excitation is characterized by a very pronounced charge transfer character and a lifetime of about 0.6 ps. When the illuminated sample is exposed to a dark relaxation period, it responds to excitation as the original dark sample, showing that photoactivation and decay of the photoactivated state are fully reversible. Thus OCP functions as a light-powered molecular switch that modulates its spectroscopic properties as a response to specific changes in light environment. We discuss the importance of this switch in cyanobacteria photoprotection and propose a mechanism wherein the red state of OCP echinenone acts as an energy dissipator via its charge transfer state. © 2012 American Chemical Society.
|Journal||Journal of Physical Chemistry B|
|Publication status||Published - 2012|