Ruffled rings: Both pyrrolidine moieties in meso‐tetraaryl‐7,8,17,18‐tetrahydroxybacteriochlorins can be sequentially expanded into morpholine rings to give the first bacteriochlorin‐like derivatives containing two non‐pyrrolic heterocycles. These porphyrioids are characterized by nonplanar conformations and significantly red‐shifted optical spectra, both of which can be modulated by the introduction of linkages between β and o‐phenyl positions.
Pulse-amplitude modulated (PAM) fluorometry is extensively used to characterize photosynthetic organisms on the slow time-scale (1–1000 s). The saturation pulse method allows determination of the quantum yields of maximal (FM) and minimal fluorescence (F0), parameters related to the activity of the photosynthetic apparatus. Also, when the sample undergoes a certain light treatment during the measurement, the fluorescence quantum yields of the unquenched and the quenched states can be determined. In the case of cyanobacteria, however, the recorded fluorescence does not exclusively stem from the chlorophyll a in photosystem II (PSII). The phycobilins, the pigments of the cyanobacterial light-harvesting complexes, the phycobilisomes (PB), also contribute to the PAM signal, and therefore, F0 and FM are no longer related to PSII only. We present a functional model that takes into account the presence of several fluorescent species whose concentrations can be resolved provided their fluorescence quantum yields are known. Data analysis of PAM measurements on in vivo cells of our model organism Synechocystis PCC6803 is discussed. Three different components are found necessary to fit the data: uncoupled PB (PBfree), PB–PSII complexes, and free PSI. The free PSII contribution was negligible. The PBfree contribution substantially increased in the mutants that lack the core terminal emitter subunits allophycocyanin D or allophycocyanin F. A positive correlation was found between the amount of PBfree and the rate constants describing the binding of the activated orange carotenoid protein to PB, responsible for non-photochemical quenching.Electronic supplementary materialThe online version of this article (doi:10.1007/s11120-015-0141-x) contains supplementary material, which is available to authorized users.
Cyanobacteria have developed responses to maintain the balance between the energy absorbed and the energy used in different pigment-protein complexes. One of the relatively rapid (a few minutes) responses is activated when the cells are exposed to high light intensities. This mechanism thermally dissipates excitation energy at the level of the phycobilisome (PB) antenna before it reaches the reaction center. When exposed to low intensities of light that modify the redox state of the plastoquinone pool, the so-called state transitions redistribute energy between photosystem I and II. Experimental techniques to investigate the underlying mechanisms of these responses, such as pulse-amplitude modulated fluorometry, are based on spectrally integrated signals. Previously, a spectrally resolved fluorometry method has been introduced to preserve spectral information. The analysis method introduced in this work allows to interpret SRF data in terms of species-associated spectra of open/closed reaction centers (RCs), (un)quenched PB and state 1 versus state 2. Thus, spectral differences in the time-dependent fluorescence signature of photosynthetic organisms under varying light conditions can be traced and assigned to functional emitting species leading to a number of interpretations of their molecular origins. In particular, we present evidence that state 1 and state 2 correspond to different states of the PB-PSII-PSI megacomplex.Electronic supplementary materialThe online version of this article (doi:10.1007/s11120-016-0248-8) contains supplementary material, which is available to authorized users.
Ultrafast time resolved emission spectra were measured in whole cells of a PSI-deficient mutant of Synechocystis sp. PCC 6803 at room temperature and at 77K to study excitation energy transfer and trapping. By means of a target analysis it was estimated that the terminal emitter of the phycobilisome, termed allophycocyanin 680, transfers its energy with a rate of (20 ps)-1 to PSII. This is faster than the intraphycobilisome energy transfer rates between a rod and a core cylinder, or between the core cylinders.
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