0000000000162662

AUTHOR

Marius Schmidt

showing 7 related works from this author

Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

2016

Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein.Science, this issue p. 725A variety of organisms have evolved mechanisms to detect and respond to light, in which the re…

0301 basic medicinePhotoreceptorsTime FactorsPhotoisomerizationLightProtein ConformationPhotochemistryPhotoreceptors MicrobialMYOGLOBINProtein structureMicrobialX-RAY-DIFFRACTIONPHOTOISOMERIZATIONMOTIONSchromophoresta116MultidisciplinarySPECTROSCOPYCrystallographyChemistryPhotochemical ProcessesTime resolved crystallographyTIMEMultidisciplinary SciencesPicosecondFemtosecondphotoactive proteinsScience & Technology - Other Topicsddc:500IsomerizationStereochemistryGeneral Science & TechnologyConjugated systemArticle03 medical and health sciencesBacterial ProteinsIsomerismEXCITATIONx-ray crystallographyPhotonsScience & TechnologyPHOTOCYCLEta114CHROMOPHOREta1182PATHWAYSChromophore030104 developmental biologyfree-electron laserssense organstrans-cis isomerization
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The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2019

Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial phytochrome at delay times of 1 ps and 10 ps after photoexcitation. The data reveal a twist of the D-ring, which leads to partial detachment of the chromophore from the protein. Unexpectedly, the conserved so-called pyrrole water is photodissociated from the chromophore, concomitant with movement of the A-ring and a key signaling aspartate. The chan…

DYNAMICSQH301-705.5ScienceEXCITED-STATEDIFFRACTION010402 general chemistryPhotosynthesisphytochromes01 natural sciencesCofactor03 medical and health scienceschemistry.chemical_compoundDeinococcus radioduransPROTON-TRANSFERREVEALSSFXCRYSTAL-STRUCTUREBiology (General)Bilin030304 developmental biologyISOMERIZATION0303 health sciencesbiologyPhytochromeD-RINGChemistryCRYSTALLOGRAPHYinitial photoresponsQRChromophore0104 chemical sciencesPhotoexcitationFemtosecondbiology.proteinBiophysics1182 Biochemistry cell and molecular biologyMedicine3111 BiomedicinevalokemiaproteiinitSignal transductionröntgenkristallografia
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Author response: The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2020

X-ray laserPrimary (chemistry)Materials sciencePhytochromebusiness.industryFemtosecondOptoelectronicsbusiness
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Linking photosynthesis and sun-induced fluorescence at sub-daily to seasonal scales

2018

Abstract Due to its close link to the photosynthetic process, sun-induced chlorophyll fluorescence (F) opens new possibilities to study dynamics of photosynthetic light reactions and to quantify CO2 assimilation rates. Although recent studies show that F is linearly related to gross primary production (GPP) on coarse spatial and temporal scales, it is argued that this relationship may be mainly driven by seasonal changes in absorbed photochemical active radiation (APAR) and less by the plant light use efficiency (LUE). In this work a high-resolution spectrometer was used to continuously measure red and far-red fluorescence and different reflectance indices within a sugar beet field during t…

010504 meteorology & atmospheric sciencesEconomicsPhotochemical reflectance index0211 other engineering and technologiesEddy covarianceGrowing seasonSoil Science02 engineering and technologyPhotochemical Reflectance IndexPhotosynthesisAtmospheric sciences01 natural sciencesFluorescence yieldSun-induced chlorophyll fluorescencemedicineddc:550Computers in Earth SciencesChlorophyll fluorescenceBiology021101 geological & geomatics engineering0105 earth and related environmental sciencesRemote sensingLight use efficiencyPhysicsDiurnal temperature variationPrimary productionGeologySeasonalitymedicine.diseaseChemistryEngineering sciences. Technology
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The three-dimensional structure of Drosophila melanogaster (6–4) photolyase at room temperature

2021

A crystal structure of a photolyase at room temperature confirms the structural information obtained from cryogenic crystallography and paves the way for time-resolved studies of the photolyase at an X-ray free-electron laser.

MECHANISMMaterials scienceAbsorption spectroscopyDNA repairfotobiologia02 engineering and technologyCrystal structureREPAIR ACTIVITY03 medical and health sciencesCOLI DNA PHOTOLYASEX-RAY-DIFFRACTIONCryptochromeStructural BiologyAnimalsserial crystallographyCRYSTAL-STRUCTURECRYPTOCHROMEPhotolyaseSERIAL FEMTOSECOND CRYSTALLOGRAPHY030304 developmental biology0303 health sciencesCrystallographyflavoproteinsFADResolution (electron density)TemperaturebanaanikärpänenDNAkidetiede(6-4) photolyase021001 nanoscience & nanotechnologyResearch PapersRADICAL TRANSFER(6–4) photolyaseroom-temperature structureCrystallographyphotolyasesDrosophila melanogasterRECONSTITUTIONX-ray crystallography1182 Biochemistry cell and molecular biologylämpötilaproteiinit0210 nano-technologyDeoxyribodipyrimidine Photo-LyasePHOTOACTIVATIONVisible spectrumActa Crystallographica Section D Structural Biology
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The hydration shell of myoglobin.

1992

The space in the unit cell of a metmyoglobin crystal not occupied by myoglobin atoms was filled with water using Monte Carlo calculations. Independent calculations with different amounts of water have been performed. Structure factors were calculated using the water coordinates thus obtained and the known coordinates of the myoglobin atoms. A comparison with experimental structure factors showed that both the low and the high resolution regime could be well reproduced with 814 Monte Carlo water molecules per unit cell with a B-value of 50 A2. The Monte Carlo water molecules yield a smaller standard R-value (0.166) than using a homogeneous electron density for the simulation of the crystal w…

Electron densityMyoglobinProtein ConformationMonte Carlo methodBiophysicsWaterGeneral MedicineCrystal structureMolecular physicsCrystalCrystallographyReciprocal latticechemistry.chemical_compoundSolvation shellMyoglobinchemistryX-Ray DiffractionYield (chemistry)Monte Carlo MethodProtein BindingEuropean biophysics journal : EBJ
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Structural basis for light control of cell development revealed by crystal structures of a myxobacterial phytochrome

2018

Phytochromes are red-light photoreceptors that were first characterized in plants, with homologs in photosynthetic and non-photosynthetic bacteria known as bacteriophytochromes (BphPs). Upon absorption of light, BphPs interconvert between two states denoted Pr and Pfr with distinct absorption spectra in the red and far-red. They have recently been engineered as enzymatic photoswitches for fluorescent-marker applications in non-invasive tissue imaging of mammals. This article presents cryo- and room-temperature crystal structures of the unusual phytochrome from the non-photosynthetic myxobacterium Stigmatella aurantiaca (SaBphP1) and reveals its role in the fruiting-body formation of this ph…

MODULE0301 basic medicinePHOTOACTIVE YELLOW PROTEINSIGNALING MECHANISMabsorption spectraMutantfotobiologiaphytochromesBiochemistryyhteyttäminenbakteeritSTIGMATELLA-AURANTIACA03 medical and health sciencesFRUITING BODY FORMATIONGeneral Materials ScienceMolecular replacementStigmatella aurantiacalcsh:ScienceUNUSUAL BACTERIOPHYTOCHROMEPHOTOCONVERSIONHistidine030102 biochemistry & molecular biologybiologyPhytochromeChemistryCRYSTALLOGRAPHYta1182photosynthetic bacteriaphotoreceptorsGeneral ChemistryChromophoreCondensed Matter Physicsbiology.organism_classification030104 developmental biologyCHROMOPHORE-BINDING DOMAINBiophysicsmyxobacterialcsh:Q3111 BiomedicinePhotosynthetic bacteriaproteiinitMOLECULAR REPLACEMENTBinding domainIUCrJ
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