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RESEARCH PRODUCT
Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein
John C. H. SpenceJennifer BrayshawDmitry MorozovThomas A. WhiteYun ZhaoRobert HenningGanesh SubramanianCornelius GatiMatthias FrankAbbas OurmazdC. HutchisonPaulraj Lourdu XavierAnton BartyOleksandr YefanovChristopher KupitzJason E. KoglinJake KoralekJesse CoeVukica ŠRajerGerrit GroenhofMarkus MetzGihan K. KetawalaMengning LiangThomas D. GrantAndrew AquilaDominik OberthuerMarius SchmidtShibom BasuUwe WeierstallPetra FrommeHenry N. ChapmanJosef S. RobinsonJasper J. Van ThorRaimund FrommeJason TenboerChelsie E. ConradKeith MoffatDaniel P. DeponteKanupriya PandeSébastien BoutetDaniel JamesNadia A. ZatsepinPeter SchwanderShatabdi Roy-chowdhurysubject
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 isomerizationdescription
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 response is mediated by protein structural changes after photon absorption. The initial step is often the photoisomerization of a conjugated chromophore. Isomerization occurs on ultrafast time scales and is substantially influenced by the chromophore environment. Here we identify structural changes associated with the earliest steps in the trans-to-cis isomerization of the chromophore in photoactive yellow protein. Femtosecond hard x-ray pulses emitted by the Linac Coherent Light Source were used to conduct time-resolved serial femtosecond crystallography on photoactive yellow protein microcrystals over a time range from 100 femtoseconds to 3 picoseconds to determine the structural dynamics of the photoisomerization reaction.
year | journal | country | edition | language |
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2016-05-06 |