0000000001000185

AUTHOR

Andreas Menzel

showing 7 related works from this author

Luminescence dynamics of hybrid ZnO nanowire/CdSe quantum dot structures

2016

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…

010302 applied physicsPhotocurrentPhotoluminescenceMaterials sciencebusiness.industryPhotoconductivityNanowire02 engineering and technologyElectronic structure021001 nanoscience & nanotechnologyCondensed Matter Physics01 natural sciencesElectron transferQuantum dot0103 physical sciencesOptoelectronics0210 nano-technologybusinessLuminescencephysica status solidi c
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Structural photoactivation of a full-length bacterial phytochrome

2016

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

Models Molecular0301 basic medicineProtein ConformationAstrophysics::High Energy Astrophysical Phenomena116 Chemical sciencesPhotoreceptors MicrobialphytochromesQuantitative Biology::Cell BehaviorStructure-Activity Relationship03 medical and health sciencesProtein structureBacterial ProteinsStructural BiologyDeinococcus radioduransBotanyResearch Articles219 Environmental biotechnologyMultidisciplinarybiologyPhytochromeHistidine kinaseta1182SciAdv r-articlesDeinococcus radioduransChromophorebiology.organism_classificationKineticsMicrosecond030104 developmental biologyStructural changephotoactivationBiophysicsPhytochromeFunction (biology)Research Article
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On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome

2018

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 …

0301 basic medicineModels MolecularCrystallography X-RayBiochemistrybakteeritProtein structurephotoconversionchromophore-binding domainTransferasestructural biologyCRYSTAL-STRUCTURETyrosineDEINOCOCCUS-RADIODURANSbiologyPhytochromeChemistryREARRANGEMENTSProtein Structure and FoldingDeinococcusmutagenesisBinding domainSignal TransductionMODULEPLANT PHYTOCHROMEPhenylalaninefotobiologia03 medical and health sciencesBacterial Proteinsprotein conformationcell signalingprotein structureBACTERIOPHYTOCHROMEMolecular BiologyX-ray crystallographysoluviestintäphytochromeAGP1BINDING DOMAINBinding Sitesta114030102 biochemistry & molecular biologyta1182Deinococcus radioduransCell BiologyChromophorebiology.organism_classificationphotoreceptor030104 developmental biologyStructural biologyFTIRBiophysicsTyrosineproteiinit3111 Biomedicineröntgenkristallografia
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Light-induced structural changes in a monomeric bacteriophytochrome

2016

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…

0301 basic medicineAllosteric regulationInfrared spectroscopyBiological Systems010402 general chemistry01 natural sciencesARTICLES03 medical and health scienceschemistry.chemical_compoundSDG 17 - Partnerships for the Goalslcsh:QD901-999[CHIM]Chemical SciencesInstrumentationSpectroscopyRadiationPhytochromebiologyChemistryMolecular biophysicsta1182/dk/atira/pure/sustainabledevelopmentgoals/partnershipsDeinococcus radioduransBiochemical ActivityCondensed Matter Physicsbiology.organism_classification0104 chemical sciences030104 developmental biologyMonomerStructural changebacterial phytochromesBiophysicslcsh:CrystallographyStructural Dynamics
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Electron tunneling from colloidal CdSe quantum dots to ZnO nanowires studied by time-resolved luminescence and photoconductivity experiments

2015

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…

PhotocurrentCondensed Matter - Materials SciencePhotoluminescenceMaterials scienceCondensed Matter - Mesoscale and Nanoscale Physicsbusiness.industryPhotoconductivityMaterials Science (cond-mat.mtrl-sci)FOS: Physical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsGeneral EnergyQuantum dotExcited stateMesoscale and Nanoscale Physics (cond-mat.mes-hall)MoleculeOptoelectronicsPhysical and Theoretical ChemistrybusinessLuminescenceQuantum tunnelling
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Signal amplification and transduction in phytochrome photosensors

2014

[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…

Models MolecularLight Signal TransductionProtein ConformationCrystallography X-RayArticleProtein structureBacterial Proteinsmolecular biophysicsDeinococcusBinding siteCalcium signalingBinding SitesMultidisciplinarybiokemiabiologyPhytochrometa1182Deinococcus radioduransChromophorebiology.organism_classificationBiochemistryBiophysicsDeinococcusPhytochromeTransduction (physiology)röntgenkristallografiaNature
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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

2017

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…

Models MolecularkinaasitentsyymitHistidine KinaseLightProtein ConformationScienceQCrystallography X-RayArticleProtein Structure SecondaryaktivointiBacterial ProteinsProtein DomainsX-Ray DiffractionphotoactivationScattering Small AngleNanotechnologysensor histidine kinasesNature Communications
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