2024
Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain
Gisriel C, Kurashov V, Iwig D, Russell B, Vinyard D, Brudvig G, Golbeck J, Lakshmi K. Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain. Science Advances 2024, 10: eadp4937. PMID: 39612342, PMCID: PMC11606441, DOI: 10.1126/sciadv.adp4937.Peer-Reviewed Original ResearchConceptsCryo-EM structureChemical bond energyElectron transfer chainBond energyPCC 6803Fuel catalystPhotosystem IBinding environmentTransfer chainLow binding affinityI variantsPlastoquinone derivativesBinding affinityCatalystPlastoquinone-9PS ICyanobacteriumBiophysical dataPhotosystemEnergyPhotonsVariantsAffinity
2021
High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803
Gisriel CJ, Wang J, Liu J, Flesher DA, Reiss KM, Huang HL, Yang KR, Armstrong WH, Gunner MR, Batista VS, Debus RJ, Brudvig GW. High-resolution cryo-electron microscopy structure of photosystem II from the mesophilic cyanobacterium, Synechocystis sp. PCC 6803. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 119: e2116765118. PMID: 34937700, PMCID: PMC8740770, DOI: 10.1073/pnas.2116765118.Peer-Reviewed Original ResearchConceptsCryo-electron microscopy structurePCC 6803Photosystem IIWater oxidationMicroscopy structureMesophilic cyanobacteriumHigh-resolution cryo-electron microscopy structuresOxygen-Evolving Photosystem IILight-driven water oxidationCyanobacterial photosystem IIHigh-resolution structuresD1 subunitPSII structureSynechocystis spLarge water channelsGenetic manipulationC-terminusBiophysical dataActive siteCyanobacteriumSpStructural pictureSubunitsOxidationWater channels
2014
Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry
Sriswasdi S, Harper SL, Tang HY, Gallagher PG, Speicher DW. Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 1801-1806. PMID: 24453214, PMCID: PMC3918770, DOI: 10.1073/pnas.1317620111.Peer-Reviewed Original ResearchConceptsMass spectrometryConformational changesStructural mass spectrometryLarge conformational rearrangementsCell membraneMembrane integrityMass spectrometry characterizationRed cell spectrinUnidentified mechanistic insightCell membrane integrityProtein complexesMacromolecular complexesDiverse functionsCell shapeBiological processesFlexible proteinsConformational rearrangementsDimer-tetramer equilibriumRed cell membraneOpen dimersCell typesΑ-spectrinKey mechanistic roleTetramerization siteBiophysical data
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