0000000000335796
AUTHOR
Andreas Menzel
Luminescence dynamics of hybrid ZnO nanowire/CdSe quantum dot structures
Colloidal CdSe quantum dots (QDs) functionalized with different organic linker molecules are attached to ZnO nanowires (NWs) to investigate the electron transfer dynamics between dots and wires. After linking the quantum dots to the nanowires, the photo-induced electron transfer (PET) from the QDs into the NWs becomes visible in the PL transients by a decrease of dot luminescence decay time. The different recombination paths inside the QDs and the PET process are discussed in the framework of a rate equation model. Photoconductivity studies confirm the electron transfer by demonstrating a strong enhancement of the wire photocurrent under light irradiation into the dot transition. (© 2016 WI…
Structural photoactivation of a full-length bacterial phytochrome
Time-resolved x-ray solution scattering reveals the conformational signaling mechanism of a bacterial phytochrome.
On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome
Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refolding of the so-called tongue extension of the phytochrome-specific GAF-related (PHY) domain of the photoreceptor. The tongue is connected to the chromophore by conserved DIP and PRXSF motifs and a conserved tyrosine, but the role of these residues in signal transduction is not clear. Here, we examine the tongue interactions and their interplay with …
Light-induced structural changes in a monomeric bacteriophytochrome
International audience; Phytochromes sense red light in plants and various microorganism. Light absorption causes structural changes within the protein, which alter its biochemical activity. Bacterial phytochromes are dimeric proteins, but the functional relevance of this arrangement remains unclear. Here, we use time-resolved X-ray scattering to reveal the solution structural change of a monomeric variant of the photosensory core module of the phytochrome from Deinococcus radiodurans. The data reveal two motions, a bend and a twist of the PHY domain with respect to the chromophore-binding domains. Infrared spectroscopy shows the refolding of the PHY tongue. We conclude that a monomer of th…
Electron tunneling from colloidal CdSe quantum dots to ZnO nanowires studied by time-resolved luminescence and photoconductivity experiments
CdSe quantum dots (QDs) with different organic linker molecules are attached to ZnO nanowires (NWs) to study the luminescence dynamics and the electron tunneling from the QDs to the nanowires in time-resolved photoluminescence (PL) and photoconductivity measurements. The PL transients of the QD luminescence indicate two different recombination channels: the direct recombination inside the QD core and the recombination via QD surface defect states. After linking the QDs to the ZnO NW surface, photo-induced electron tunneling from an excited state of the QD into the conduction band of the nanowire becomes visible by a clear decrease of the PL decay time. Efficient electron tunneling is confir…
Signal amplification and transduction in phytochrome photosensors
[Introduction] Page 2 of 20 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 cell ular functions in plants, bacteria, and fungi. 1-9 Bacterial phytochro mes consist of a photosensory core and a C-te rminal regulatory domain. 10,11 Structures of photosensory cores are reported in the resting state 12-18 and conformational responses to light activat ion have been proposed in the vicinity of the chromophore. 19-23 However, the structure of the signalling state and the mechanism of downstream signal re lay through the photosensory core remain e…
Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a t…