• Energy Research

Coherence in Photosynthesis It is unclear how energy absorbed by pigments in antenna proteins is transferred to the central site of chemical catalysis during photosynthesis. Hildner et al. (p. 1448 ) observed coherence—prolonged persistence of a quantum mechanical phase relationship—at the single-molecule level in light-harvesting complexes from purple bacteria. The results bolster conclusions from past ensemble measurements that coherence plays a pivotal role in photosynthetic energy transfer. Hayes et al. (p. 1431 , published online 18 April) examined a series of small molecules comprised of bridged chromophores that also manifest prolonged coherence.

The accumulation of organic co-solvents in cells is a basic strategy for organisms from various species to increase stress tolerance in extreme environments. Widespread representatives of this class of co-solvents are trimethylamine-N-oxide (TMAO) and betaine; these small molecules are able to stabilize the native conformation of proteins and prevent their aggregation. Despite their importance, detailed experimental studies on the impact of these co-solvents on the energy landscape of proteins have not yet been carried out. We use single-molecule spectroscopy at cryogenic temperatures to examine the influence of these physiological relevant co-solvents on photosystem I (PSI) from Thermosynechococcus elongatus. In contrast to PSI ensemble spectra, which are almost unaffected by the addition of TMAO and betaine, statistical analysis of the fluorescence emission from individual PSI trimers yields insight into the interaction of the co-solvents with PSI. The results show an increased homogeneity upon addition of TMAO or betaine. The number of detectable zero-phonon lines (ZPLs) is reduced, indicating spectral diffusion processes with faster rates. In the framework of energy landscape model these findings indicate that co-solvents lead to reduced barrier heights between energy valleys, and thus efficient screening of protein conformations can take place.

Strong anticorrelation between the fluorescence emission of different emitters is observed by employing single-molecule fluorescence spectroscopy on photosystem I at cryogenic temperatures. This anticorrelation demonstrates a time-dependent interaction between pigments participating in the exciton transfer chain, implying that uniquely defined energy transfer pathways within the complex do not exist. Fluctuations of the chromophores themselves or their immediate protein surroundings induce changes in their site energy, and, as a consequence, these fluctuations change the coupling within the excitation transfer pathways. The time scales of the site energy fluctuations of the individual emitters do not meet the time scales of the observed correlated emission behavior. Therefore, the emitters must be fed individually by energetically higher lying states, causing the observed intensity variations. This phenomenon is shown for photosystem I pigment–protein complexes from 2 different cyanobacteria ( Thermosynechococcus elongatus and Synechocystis sp. PCC 6803) with strongly different spectral properties underlining the general character of the findings. The variability of energy transfer pathways might play a key role in the extreme robustness of light-harvesting systems in general.

Room-temperature studies of single molecules at femtosecond timescales provide detailed observation and control of ultrafast electronic and vibrational dynamics of organic dyes and photosynthetic complexes, probing quantum dynamics at ambient conditions and elucidating its role in chemistry and biology.