Charge transfer states in phycobilisomes

Phycobilisomes (PBs) absorb light and supply downstream photosynthetic processes with excitation energy in many cyanobacteria and algae. In response to a sudden increase in light intensity, excess excitation energy is photoprotectively dissipated in PBs by means of the orange carotenoid protein (OCP)-related mechanism or via a light-activated intrinsic decay channel. Recently, we have identified that both mechanisms are associated with far-red emission states. Here, we investigate the far-red states involved with the light-induced intrinsic mechanism by exploring the energy landscape and electro-optical properties of the pigments in PBs. While Stark spectroscopy showed that the far-red states in PBs exhibit a strong charge-transfer (CT) character at cryogenic temperatures, single molecule spectroscopy revealed that CT states should also be present at room temperature. Owing to the strong environmental sensitivity of CT states, the knowledge gained from this study may contribute to the design of a new generation of fluorescence markers

Stark fluorescence spectroscopy on peridinin–chlorophyll–protein complex of dinoflagellate, Amphidinium carterae

Because of their peculiar but intriguing photophysical properties, peridinin–chlorophyll–protein complexes (PCPs), the peripheral light-harvesting antenna complexes of photosynthetic dinoflagellates have been unique targets of multidimensional theoretical and experimental investigations over the last few decades. The major light-harvesting chlorophyll a (Chl a) pigments of PCP are hypothesized to be spectroscopically heterogeneous. To study the spectral heterogeneity in terms of electrostatic parameters, we, in this study, implemented Stark fluorescence spectroscopy on PCP isolated from the dinoflagellate Amphidinium carterae. The comprehensive theoretical modeling of the Stark fluorescence spectrum with the help of the conventional Liptay formalism revealed the simultaneous presence of three emission bands in the fluorescence spectrum of PCP recorded upon excitation of peridinin. The three emission bands are found to possess different sets of electrostatic parameters with essentially increasing magnitude of charge-transfer character from the blue to redder ones. The different magnitudes of electrostatic parameters give good support to the earlier proposition that the spectral heterogeneity in PCP results from emissive Chl a clusters anchored at a different sites and domains within the protein network

A new model for magnetoreception

Certain migratory birds can sense the earth's magnetic field. The nature of this process is not yet properly understood. Here we offer a simple explanation according to which birds literally `see' the local magnetic field: Our model relates the well-established radical pair hypothesis to the phenomenon of Haidinger's brush, a capacity to see the polarisation of light. This new picture explains recent surprising experimental data indicating long lifetimes for the radical pair. Moreover there is a clear evolutionary path toward this field sensing mechanism: it is an enhancement of a weak effect that may be present in many species.Comment: 8 pages, 5 figures, version of final published pape

The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll proteins

Understanding how specific protein environments affect the mechanisms of non-radiative energy dissipation within densely assembled chlorophylls in photosynthetic protein complexes is of great interest to the construction of bioinspired solar energy conversion devices. Mixing of charge-transfer and excitonic states in excitonically interacting chlorophylls was implicated in shortening excited states lifetimes, but its relevance to active control of energy dissipation in natural systems is under considerable debate. Here we show that the degree of fluorescence quenching in two similar pairs of excitonically interacting bacteriochlorophyll derivatives is directly associated with increasing charge-transfer character in the excited state, and that the protein environment may control non-radiative dissipation by affecting the mixing of charge-transfer and excitonic states. The capability of local protein environments to determine the fate of excited states, and thereby to confer different functionalities to excitonically coupled dimers substantiates the dimer as the basic functional element of photosynthetic enzymes

Identification of two emitting sites in the dissipative state of the major light harvesting antenna

In order to cope with the deleterious effects of excess light, photosynthetic organisms have developed remarkable strategies where the excess energy is dissipated as heat by the antenna system. In higher plants one main player in the process is the major light harvesting antenna of Photosystem II (PSII), LHCII. In this paper we applied Stark fluorescence spectroscopy to LHCII in different quenching states to investigate the possible contribution of charge-transfer states to the quenching. We find that in the quenched state the fluorescence displays a remarkable sensitivity to the applied electric field. The resulting field-induced emission spectra reveal the presence of two distinct energy dissipating sites both characterized by a strong but spectrally very different response to the applied electric field. We propose the two states to originate from chlorophyll-chlorophyll and chlorophyll-carotenoid charge transfer interactions coupled to the chlorophyll exciton state in the terminal emitter locus and discuss these findings in the light of the different models proposed to be responsible for energy dissipation in photosynthesis. © 2011 The Owner Societies