The excess oxygen concentration in the photosynthetic membranes of functioning oxygenic photosynthetic cells was estimated using classical diffusion theory combined with experimental data on oxygen production rates of cyanobacterial cells. The excess oxygen concentration within the plesiomorphic cyanobacterium Gloeobactor violaceus is only 0.025 μM, or four orders of magnitude lower than the oxygen concentration in air-saturated water. Such a low concentration suggests that the first oxygenic photosynthetic bacteria in solitary form could have evolved ∼2.8 billion years ago without special mechanisms to protect them against reactive oxygen species. These mechanisms instead could have been developed during the following ∼500 million years while the oxygen level in the Earth's atmosphere was slowly rising. Excess oxygen concentrations within individual cells of the apomorphic cyanobacteria Synechocystis and Synechococcus are 0.064 and 0.25 μM, respectively. These numbers suggest that intramembrane and intracellular proteins in isolated oxygenic photosynthetic cells are not subjected to excessively high oxygen levels. The situation is different for closely packed colonies of photosynthetic cells. Calculations show that the excess concentration within colonies that are ∼40 μm or larger in diameter can be comparable to the oxygen concentration in air-saturated water, suggesting that species forming colonies require protection against reactive oxygen species even in the absence of oxygen in the surrounding atmosphere.

The fate of triplet excited states in the Fenna-Matthew-Olson (FMO) pigment-protein complex is studied by means of time-resolved nanosecond spectroscopy and exciton model simulations. Experiments reveal microsecond triplet excited-state energy transfer between the bacteriochlorophyll (BChl) pigments, but show no evidence of triplet energy transfer to molecular oxygen, which is known to produce highly reactive singlet oxygen and is the leading cause of photo damage in photosynthetic proteins. The FMO complex is exceptionally photo stable despite the fact it contains no carotenoids, which could effectively quench triplet excited states of (bacterio)chlorophylls and are usually found within pigment-protein complexes. It is inferred that the triplet excitation is transferred to the lowest energy pigment, BChl 3, within the FMO complex, whose triplet state energy is shifted by pigment-protein interactions below that of the singlet oxygen excitation. Thus, the energy transfer to molecular oxygen is blocked and the FMO does not need carotenoids for photo protection.

Plants can safely dissipate excess excitation energy during light harvesting to prevent the formation of triplet chlorophyll, which can generate deleterious singlet oxygen. With this regulation, known as non-photochemical quenching

The earliest steps in bacterial photosynthesis require that an antenna system efficiently capture incident photons and shuttle the excitation energy to the ''special pair'' bacteriochlorophylls within the membrane-bound reaction center where charge separation occurs. Previous work has shown coherent energy transfer-a wavelike transfer process-among peripheral chromophores, bacteriopheophytins and accessory bacteriochlorophylls, at cryogenic temperatures. Whether or not this coherent transfer extends to the special pair, however, has remained elusive at any temperature. Here we report direct evidence that the special pair is coherently coupled to the accessory bacteriochlophylls and that this coherence dephases only upon transfer to the special pair-the maximal amount of coherence physically possible. We employ Gradient Assisted Photon Echo Spectroscopy to simultaneously excite the bacteriopheophytins, accessory bacteriochlorophylls and the special pair in the reaction center from Rhodobacter sphaeroides. These results suggest the bacteria exploits coherent energy transfer at room temperature.