Sensory proteins must relay structural signals from the sensory site over large distances to regulatory output domains. Phytochromes are a major family of red-light sensing kinases that control diverse cellular functions in plants, bacteria, and fungi.1-9 Bacterial phytochromes consist of a photosensory core and a C-terminal regulatory domain.10,11 Structures of photosensory cores are reported in the resting state12-18 and conformational responses to light activation have been proposed in the vicinity of the chromophore.19-23 However, the structure of the signalling state and the mechanism of downstream signal relay through the photosensory core remain elusive. Here, we report crystal and solution structures of the resting and active states of the photosensory core of the bacteriophytochrome from Deinococcus radiodurans. The structures reveal an open and closed form of the dimeric protein for the signalling and resting state, respectively. This nanometre scale rearrangement is controlled by refolding of an evolutionarily conserved “tongue”, which is in contact with the chromophore. The findings reveal an unusual mechanism where atomic scale conformational changes around the chromophore are first amplified into an Ångström scale distance change in the tongue, and further grow into a nanometre scale conformational signal. The structural mechanism is a blueprint for understanding how the sensor proteins connect to the cellular signalling network.

All-inorganic colloidal perovskite quantum dots (QDs) based on cesium, lead, and halide have recently emerged as promising light emitting materials. CsPbBr QDs have also been demonstrated as stable two-photon-pumped lasing medium. However, the reported two photon absorption (TPA) cross sections for these QDs differ by an order of magnitude. Here we present an in-depth study of the TPA properties of CsPbBr QDs with mean size ranging from 4.6 to 11.4 nm. By using femtosecond transient absorption (TA) spectroscopy we found that TPA cross section is proportional to the linear one photon absorption. The TPA cross section follows a power law dependence on QDs size with exponent 3.3 ± 0.2. The empirically obtained power-law dependence suggests that the TPA process through a virtual state populates exciton band states. The revealed power-law dependence and the understanding of TPA process are important for developing high performance nonlinear optical devices based on CsPbBr nanocrystals.

Due to their superior photoluminescence (PL) quantum yield (QY) and tunable optical band gap, all-inorganic CsPbBr3 perovskite quantum dots (QDs) have attracted intensive attention for the application in solar cells, light emitting diodes (LED), photodetectors and laser devices. In this scenario, the stability of such materials becomes a critical factor to be revealed. We hereby investigated the long-term stability of as-synthesized CsPbBr3 QDs suspended in toluene at various environmental conditions. We found light illumination would induce drastic photo-degradation of CsPbBr3 QDs. The steady-state spectroscopy, transmission electron microscopy (TEM), and X-ray diffraction (XRD) verified that CsPbBr3 QDs tend to aggregate to form larger particles under continuous light soaking. In addition, decreasing PL QY of the QDs during light soaking indicates the formation of trap sites. Our work reveals that the main origin of instability in CsPbBr3 QDs and provides reference to engineer such QDs towards optimal device application.

Time-resolved x-ray solution scattering reveals the conformational signaling mechanism of a bacterial phytochrome.

Background: Near-infrared (NIR) fluorescent bacteriophytochromes are valuable for optical imaging in mammals. Results: Reversal of one position in the fluorescent phytochrome variant IFP1.4 led to the brightest monomeric NIR phytofluor known. Conclusion: Crystallography shows that limiting motion and changing polarity in the chromophore binding pocket increase fluorescence. Significance: Understanding the source of increased fluorescence in NIR fluorescent phytofluors is essential for further improving these novel imaging tools.

Injection of an electron from the excited dye molecule to the semiconductor is the initial charge separation step in dye-sensitized solar cells (DSC's). Though the dynamics of the forward injection process has been widely studied, the results reported so far are controversial, especially for complete DSC's. In this work, the electron injection in titanium dioxide (TiO 2 ) films sensitized with ruthenium bipyridyl dyes N3 and N719 was studied both in neat solvent and in a typical iodide/triiodide (I − /I 3 − ) DSC electrolyte. Transient absorption (TA) spectroscopy was used to monitor both the formation of the oxidized dye and the arrival of injected electrons to the conduction band of TiO 2 . Emission lifetime of the dye-sensitized films was recorded with time-correlated single photon counting to reveal nanosecond time scales of injection. It was found that the injection dynamics of the N3 and N719 dyes are similar. In solvent the injection from both dyes occurs in the femto-to picosecond time scale while in the I − /I 3 − electrolyte, it slows down significantly, extending to the nanosecond time domain. The presence of the electrolyte was found to increase the excited state lifetime of the dyes, implying that injection efficiency remains high despite the slower kinetics of injection compared to neat solvent. A remarkable new finding was that the prominent absorption signal of the oxidized dye observed in neat solvent vanished almost completely in the presence of the electrolyte, while the arrival of electrons to the conduction band of TiO 2 was practically unaltered, only slowed down. The observed disappearance of the oxidized dye population in the I − /I 3 − electrolyte is most likely related to the reduction of the oxidized dye by iodide I − , which is the first step of the dye regeneration process. To the best of our knowledge, this is the first time initial dye regeneration has been shown to occur in a few picoseconds after injection.

Photoinduced processes in phthalocyanine-functionalized gold nanoparticles (Pc-AuNPs) have been investigated by spectroscopic measurements. The metal-free phthalocyanines used have two linkers with thioacetate groups for bonding to the gold nanoparticle surface, and the attachment was achieved using a ligand exchange reaction. The absorption spectrum of the Pc-AuNPs shows a broadening of the phthalocyanine Q-band absorption, probably due to a tight packing of the phthalocyanines on the gold nanoparticle surface. For the attached phthalocyanines, fluorescence is strongly quenched, and the fluorescence lifetimes determined by time-correlated single photon counting (TCSPC) are strongly reduced. The quenching mechanisms were studied in detail with time-resolved absorption (pump−probe) measurements. A selective excitation of the gold cores in the pump−probe experiment results in an energy transfer from the gold nanoparticles to the attached phthalocyanines in ∼2.4 ps. Photoexcitation of mainly the phthalocyanines in the functionalized nanoparticles leads to an electron transfer to the gold core in ∼3.0 ps. The recombination of charges in the Pc-AuNP takes place on a picosecond time scale. In addition, there is evidence of energy transfer from the photoexcited phthalocyanines to the gold nanoparticles.

Phytochrome proteins regulate many photoresponses of plants and microorganisms. Light absorption causes isomerization of the biliverdin chromophore, which triggers a series of structural changes to activate the signaling domains of the protein. However, the structural changes are elusive, and therefore the molecular mechanism of signal transduction remains poorly understood. Here, we apply two-color step-scan infrared spectroscopy to the bacteriophytochrome from Deinococcus radiodurans. We show by recordings in HO and DO that the hydrogen bonds to the biliverdin D-ring carbonyl become disordered in the first intermediate (Lumi-R) forming a dynamic microenvironment, then completely detach in the second intermediate (Meta-R), and finally reform in the signaling state (Pfr). The spectra reveal via isotope labeling that the refolding of the conserved "PHY-tongue" region occurs with the last transition between Meta-R and Pfr. Additional changes in the protein backbone are detected already within microseconds in Lumi-R. Aided by molecular dynamics simulations, we find that a strictly conserved salt bridge between an arginine of the PHY tongue and an aspartate of the chromophore binding domains is broken in Lumi-R and the arginine is recruited to the D-ring C═O. This rationalizes how isomerization of the chromophore is linked to the global structural rearrangement in the sensory receptor. Our findings advance the structural understanding of phytochrome photoactivation.