Down to a mutual center-to-center distance R between pigments of

Down to a mutual center-to-center distance R between pigments of 1.5 nm, the transfer rate

scales with R −6 according to the Förster equation whereas as shorter distances excitonic effects start to play a major role and excitations start to become more and more delocalized over the different pigments (see, e.g., van Amerongen et al. (2000)). However, if the pigments are getting too MLN2238 close, then an unwanted secondary effect called concentration quenching may occur, leading to a shortening of the excited-state lifetime, thereby decreasing the quantum efficiency (Beddard and Porter 1976). Very roughly, PSI of plants can be approximated by a cylinder of 12-nm diameter and 5-nm height, containing 170 Chls. This means that the pigment concentration in this system is 0.5 M. The excited-state lifetime of a diluted solution of Chls is around 6 ns, but it is below 100 ps at 0.5 M in lipid vesicles (Beddard et al. 1976). Apparently, PSI is able to avoid concentration quenching to keep the quantum efficiency close to 1. What is the trick? It is the protein that keeps the pigments at the correct distance and geometry to facilitate fast energy transfer and to prevent

excited-state quenching. In addition, the protein has a role in tuning the energy levels of the pigments (defining at which wavelength/color the maximum absorption occurs) whereas its vibrations (phonons) PLX4032 can couple to the electronic transitions of the pigments to broaden the absorption spectra and to allow energy transfer (both uphill and downhill) through the excited-state energy landscape (Van Amerongen et al. 2000). But this is not yet all. When one reads about the energy transfer efficiency, it is nearly always written that EET should follow

an energy gradient (from high-energy pigments Sitaxentan to low-energy ones) to be efficient. Indeed, the picture used to exemplify photosynthetic energy transfer is commonly a deep funnel, where the energy is transferred between pigments of colors throughout the whole rainbow to end up on the primary donor which is the pigment with the lowest excited-state energy. This picture fits rather well with the antennae of cyanobacteria, the phycobilisomes, but it is clearly not a realistic this website representation of the situation in plants and green algae in which the most of the pigments are more or less isoenergetic. While it is correct for PSI that the primary electron donor (absorbing around 700 nm) is lower in energy than the bulk pigments (the maximum absorption of PSI is at 680 nm), it is also true that almost all PSI complexes contain Chls that absorb at energies below that of the primary donor, and they are responsible for the so-called red forms (Karapetyan 2006; Brecht et al. 2009). It was already shown in Croce et al.

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