2023
Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium
Gisriel C, Elias E, Shen G, Soulier N, Flesher D, Gunner M, Brudvig G, Croce R, Bryant D. Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium. Science Advances 2023, 9: eadg0251. PMID: 36961897, PMCID: PMC10038336, DOI: 10.1126/sciadv.adg0251.Peer-Reviewed Original ResearchConceptsFar-red lightLight-harvesting proteinsLight-harvesting phycobiliproteinsCryo-electron microscopyStructure-function relationshipsLow-light environmentsAP complexesThermophilic cyanobacteriumLow lightBiological plasticityPhotosystem I.Likely associatesAllophycocyaninParalogsEnhanced abilityCyanobacteriaCyanobacteriumAcclimationSubunitsPhycobiliproteinsProteinResource accessibilityDiversityAssemblesChlorophyll
2022
Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light
Gisriel C, Shen G, Flesher D, Kurashov V, Golbeck J, Brudvig G, Amin M, Bryant D. Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light. Journal Of Biological Chemistry 2022, 299: 102815. PMID: 36549647, PMCID: PMC9843442, DOI: 10.1016/j.jbc.2022.102815.Peer-Reviewed Original ResearchConceptsFar-red light photoacclimationChl dFar-red lightPhotosystem IIChl fWater-splitting enzymeEnergy transferDimeric photosystem II complexesCryo-EM structurePhotosystem II complexElectron transfer chainWater oxidationChl f moleculesDimeric complexStructure-function relationshipsPhotosynthetic machineryPsbH subunitProtein environmentMonomeric structureOxygenic photosynthesisVisible lightFormyl moietyF moleculesAccessory pigmentsTransfer chain
2005
Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*
Bautista J, Tracewell C, Schlodder E, Cunningham F, Brudvig G, Diner B. Construction and Characterization of Genetically Modified Synechocystis sp. PCC 6803 Photosystem II Core Complexes Containing Carotenoids with Shorter π-Conjugation than β-Carotene*. Journal Of Biological Chemistry 2005, 280: 38839-38850. PMID: 16159754, DOI: 10.1074/jbc.m504953200.Peer-Reviewed Original ResearchMeSH KeywordsBeta CaroteneCarotenoidsCationsChlorophyllChromatographyChromatography, High Pressure LiquidElectronsGene DeletionLightManganeseModels, ChemicalModels, MolecularMutationOxidation-ReductionOxidoreductasesOxygenPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPigmentationRhodobacter capsulatusSpectrophotometrySpectrophotometry, InfraredSynechocystisTemperatureTime FactorsTyrosineConceptsPhytoene desaturase geneII core complexesDesaturase genePS II core complexesSynechocystis spCore complexPS II assemblyCarotene desaturase genePhotosystem II core complexPCC 6803Rhodobacter capsulatusWild typeMutant strainRedox functionPhotosystem IISecondary electron transfer pathwayGenesElectron transfer pathwayLight-induced formationCarotenoidsSpChlorophyllConjugated pi-electron systemPathwayComplexes
2004
Q-Band EPR of the S2 State of Photosystem II Confirms an S=5/2 Origin of the X-Band g=4.1 Signal
Haddy A, Lakshmi K, Brudvig G, Frank H. Q-Band EPR of the S2 State of Photosystem II Confirms an S=5/2 Origin of the X-Band g=4.1 Signal. Biophysical Journal 2004, 87: 2885-2896. PMID: 15454478, PMCID: PMC1304705, DOI: 10.1529/biophysj.104.040238.Peer-Reviewed Original ResearchConceptsSame spin systemS2 stateSpin systemsZero-field splitting valuesMiddle Kramers doubletPhotosystem IILight-induced signalsS2 oxidation stateX-bandKramers doubletX-band signalQ-band EPRPSII-enriched membrane fragmentsSplitting valuesLow-field signalMn clusterQ-bandState originEPR signalOxidation stateStateDoubletSpectraSignalsGHz
2001
Carotenoid Photooxidation in Photosystem II
Tracewell C, Vrettos J, Bautista J, Frank H, Brudvig G. Carotenoid Photooxidation in Photosystem II. Archives Of Biochemistry And Biophysics 2001, 385: 61-69. PMID: 11361027, DOI: 10.1006/abbi.2000.2150.Peer-Reviewed Original ResearchConceptsPhotosystem IIElectron transfer reactionsPhotosynthetic reaction centersWater oxidationLight-harvesting pigmentsCarotenoid cationOxidizing intermediatesElectron transferRedox roleBacterial photosynthesisReaction centersPhysical methodsCationsPhotooxidationCarotenoid compositionRedoxOxidationIntermediatesAlternate pathwayCarotenoidsMinireviewReactionPhotoprotectionPossible rolePigments
1998
Catalase-Free Photosystem II: The O2-Evolving Complex Does Not Dismutate Hydrogen Peroxide †
Sheptovitsky Y, Brudvig G. Catalase-Free Photosystem II: The O2-Evolving Complex Does Not Dismutate Hydrogen Peroxide †. Biochemistry 1998, 37: 5052-5059. PMID: 9548736, DOI: 10.1021/bi972872s.Peer-Reviewed Original Research
1997
Fluorescence Quenching by Chlorophyll Cations in Photosystem II †
Schweitzer R, Brudvig G. Fluorescence Quenching by Chlorophyll Cations in Photosystem II †. Biochemistry 1997, 36: 11351-11359. PMID: 9298954, DOI: 10.1021/bi9709203.Peer-Reviewed Original ResearchConceptsFluorescence quenchingPhotosystem IIElectron donorDonor sideElectron paramagnetic resonance spectroscopyRedox-active tyrosinesRedox-active centersCharge-separated stateSteady-state fluorescence quenchingParamagnetic resonance spectroscopyRedox-active componentsElectron donor sideElectron transfer pathwayCytochrome b559Redox stateFluorescence intensityO2-evolving complexPrimary electron donorReversible oxidationChlorophyll cationElectron donationFurther oxidationChlZRapid photooxidationDifferent sample preparation
1994
Location of chlorophyllZ in photosystem II.
Koulougliotis D, Innes J, Brudvig G. Location of chlorophyllZ in photosystem II. Biochemistry 1994, 33: 11814-22. PMID: 7918399, DOI: 10.1021/bi00205a018.Peer-Reviewed Original ResearchBacteriochlorophyllsChlorophyllCold TemperatureCyanidesDarknessDysprosiumEdetic AcidElectron Spin Resonance SpectroscopyIronLightLight-Harvesting Protein ComplexesManganeseMicrowavesModels, ChemicalOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpinacia oleracea
1992
Photooxidation of cytochrome b559 in oxygen-evolving photosystem II.
Buser C, Diner B, Brudvig G. Photooxidation of cytochrome b559 in oxygen-evolving photosystem II. Biochemistry 1992, 31: 11449-59. PMID: 1445880, DOI: 10.1021/bi00161a025.Peer-Reviewed Original ResearchConceptsCyt b559Photosystem II protein complexDark reductionOptical spectroscopyElectron transfer kineticsOxygen-evolving photosystem IIPSII-enriched membranesCytochrome b559Redox stateS2QA- charge recombinationExtent of photooxidationRate of photooxidationPrimary electron acceptorPH range 5.0Plastoquinone poolPSII samplesAcidic pH valuesRoom temperatureElectron acceptorPhotosystem IIPhotooxidationRate of reductionRedox equilibriumRange 5.0P680
1989
Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680.
Metz J, Nixon P, Rögner M, Brudvig G, Diner B. Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680. Biochemistry 1989, 28: 6960-9. PMID: 2510819, DOI: 10.1021/bi00443a028.Peer-Reviewed Original Research
1985
Electron transfer in photosystem II at cryogenic temperatures.
De Paula J, Innes J, Brudvig G. Electron transfer in photosystem II at cryogenic temperatures. Biochemistry 1985, 24: 8114-20. PMID: 3004575, DOI: 10.1021/bi00348a042.Peer-Reviewed Original ResearchConceptsS2-state multiline EPR signalMultiline EPR signalElectron donationEPR signalS1 stateCytochrome b559Electron paramagnetic resonance spectroscopyParamagnetic resonance spectroscopyStable charge separationPhotosystem IIChemical oxidationChlorophyll cationElectron transferReaction center concentrationCharge separationElectron donorResonance spectroscopyS2 stateReaction centersTemperature rangeP680Signal speciesCenter concentrationB559Donation pathwayActive and resting states of the O2-evolving complex of photosystem II.
Beck W, De Paula J, Brudvig G. Active and resting states of the O2-evolving complex of photosystem II. Biochemistry 1985, 24: 3035-43. PMID: 2990539, DOI: 10.1021/bi00333a035.Peer-Reviewed Original ResearchConceptsO2-evolving complexEPR signalPSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyPhotosystem IIElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalParamagnetic resonance spectroscopyS2 state EPR signalsMn sitesMultiline EPR signalSpinach photosystem IIThylakoid membranesCatalytic reductionChemical propertiesResonance spectroscopyDifferent hyperfine structureO2