It appears that in the end all Lhca’s transfer a similar amount of excitations to the core (Wientjes et al. 2011b). To directly check the influence of the red forms on the trapping time, Wientjes et al. also measured a PSI-LHCI complex which is identical to that of the WT but in which Lhca4 had been substituted with Lhca5 GSK1838705A purchase that does not contain red forms. The fastest decay component becomes slower in the presence of Lhca5 (it goes from 20 to 26 ps), but the corresponding amplitude is strongly increased as compared to WT PSI

(with Lhca4), whereas the amplitude of the slow component, which corresponds to a red spectrum, has concomitantly decreased. This clearly indicates that the transfer from the “blue” antenna Lhca5 to the core is extremely fast. This experiment also shows that the fast decay

component commonly seen in the EET MI-503 in vivo measurements of PSI, is not only due to the trapping from the core, but also from the “blue” antennae. The slow decay originates from Lhca4 and Lhca3. The data show that these red forms together slow down the transfer by a factor of two, in agreement with previous suggestions (Engelmann et al. 2006; Slavov et al. 2008). A scheme of the energy transfer in PSI-LHCI based on Wientjes et al. (2011b) is shown in Fig. 4. Fig. 4 Schematic presentations of energy transfer and trapping in PSI-LHCI based on Wientjes et al. (2011b).

Increasing thickness of the arrows indicates selleck inhibitor increasing rates. The transfer rate between Lhca2 and Lhca4 could not be estimated from the target analysis in that study, but based on structural data, it has been suggested to be similar to the Farnesyltransferase intradimer transfer rates In conclusion, PSI-LHCI in plants the trapping time is around 50 ps. The most red forms are associated with the outer antenna. All Lhca’s transfer excitation energy to the core, the blue Lhca’s (1 and 2) very rapidly and the red ones (Lhca3 and 4) somewhat slower. PSI-LHCI-LHCII supercomplex In all conditions in which PSII is preferentially excited, part of the LHCII population moves to PSI to increase its antenna size, forming the PSI-LHCI-LHCII supercomplex (e.g., Lemeille and Rochaix 2010). This is considered to be a short-term acclimation mechanism that allows maintaining the excitation balance between the two photosystems upon rapid changes in light quality/quantity. However, it has recently been shown that the association of LHCII to PSI occurs also upon long-term acclimation, and it is in fact the most common state in A. thaliana (Wientjes et al. 2013). In normal light conditions (100 μmol/photons/m2) around 50 % of the PSI complexes is complemented by one LHCII trimer, while this value increases in low light and decreases in high light.