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
2008
Quantum Mechanics/Molecular Mechanics Study of the Catalytic Cycle of Water Splitting in Photosystem II
Sproviero EM, Gascón JA, McEvoy JP, Brudvig GW, Batista VS. Quantum Mechanics/Molecular Mechanics Study of the Catalytic Cycle of Water Splitting in Photosystem II. Journal Of The American Chemical Society 2008, 130: 3428-3442. PMID: 18290643, DOI: 10.1021/ja076130q.Peer-Reviewed Original ResearchConceptsSubstrate water moleculesWater moleculesMu-oxo bridgeOxygen-evolving complexWater splittingQuantum mechanics/molecular mechanics (QM/MM) hybrid methodsQuantum Mechanics/Molecular Mechanics StudySolar fuel production systemsPhotosystem IIX-ray diffraction structureMolecular mechanics studySecond coordination shellCyanobacterium Thermosynechococcus elongatusOxomanganese clusterDioxygen evolutionTerminal ligandsXRD structureCatalytic clustersCP43-R357Ligand exchangeCatalytic reactionCatalytic cycleReaction intermediatesS0 stateNucleophilic attack
2005
Resonance Raman spectroscopy of carotenoids in Photosystem II core complexes
Tracewell C, Cua A, Bocian D, Brudvig G. Resonance Raman spectroscopy of carotenoids in Photosystem II core complexes. Photosynthesis Research 2005, 83: 45-52. PMID: 16143906, DOI: 10.1007/s11120-004-2350-6.Peer-Reviewed Original ResearchMeSH KeywordsCarotenoidsCyanobacteriaPhotosystem II Protein ComplexSpectrum Analysis, RamanTemperatureConceptsII core complexesPhotosystem II core complexResonance Raman spectroscopyPS II core complexesRaman spectroscopyTrans configurationSecondary electron transfer reactionsElectron transfer reactionsMolecular wiresNeutral carotenoidsRR spectraAbsorption bandsCore complexDifference experimentsReaction centersExcitation wavelengthComplexesSpectroscopyPS IIRR resultsReactionΒ-caroteneSpectraCarotenoidsConfiguration
2003
Two Redox-Active β-Carotene Molecules in Photosystem II †
Tracewell C, Brudvig G. Two Redox-Active β-Carotene Molecules in Photosystem II †. Biochemistry 2003, 42: 9127-9136. PMID: 12885246, DOI: 10.1021/bi0345844.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, PhysiologicalBeta CaroteneCyanobacteriaDarknessElectron Spin Resonance SpectroscopyFree RadicalsFreezingLight-Harvesting Protein ComplexesNormal DistributionOxidation-ReductionPhotochemistryPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectroscopy, Near-InfraredSpinacia oleraceaTyrosineConceptsSecondary electron transfer pathwayElectron transfer pathwayElectron paramagnetic resonance spectroscopyElectron transfer reactionsElectron transfer pathParamagnetic resonance spectroscopyHole-hopping mechanismPS II core complexesΒ-carotene moleculesPS II membranesII core complexesPhotosystem IIIR spectroscopyPS IILow temperatureCharge separationElectrostatic interactionsOxygen evolutionResonance spectroscopyLow-temperature illuminationInhibited samplesSpectroscopyEquilibrated statePeak variesSynechocystis PCC 6803The X‐ray structure of photosystem II reveals a novel electron transport pathway between P680, cytochrome b 559 and the energy‐quenching cation, ChlZ +
Vasil’ev S, Brudvig G, Bruce D. The X‐ray structure of photosystem II reveals a novel electron transport pathway between P680, cytochrome b 559 and the energy‐quenching cation, ChlZ +. FEBS Letters 2003, 543: 159-163. PMID: 12753925, DOI: 10.1016/s0014-5793(03)00442-3.Peer-Reviewed Original ResearchPulsed High-Frequency EPR Study on the Location of Carotenoid and Chlorophyll Cation Radicals in Photosystem II
Lakshmi K, Poluektov O, Reifler M, Wagner A, Thurnauer M, Brudvig G. Pulsed High-Frequency EPR Study on the Location of Carotenoid and Chlorophyll Cation Radicals in Photosystem II. Journal Of The American Chemical Society 2003, 125: 5005-5014. PMID: 12708850, DOI: 10.1021/ja0295671.Peer-Reviewed Original ResearchMeSH KeywordsBeta CaroteneBinding SitesCationsChlorophyllCyanobacteriaDeuteriumElectron Spin Resonance SpectroscopyFerrous CompoundsFree RadicalsLight-Harvesting Protein ComplexesOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein ConformationRhodospirillumConceptsHigh-frequency EPR spectroscopyRelaxation enhancementEPR spectroscopyRelaxation ratePS IIElectron donorChlorophyll cation radicalsSpin-lattice relaxation rateWater oxidation complexFrequency EPR StudyPigment-protein complexesPhotosystem IIGreater relaxation enhancementCarotenoid-binding siteCation radicalsChlorophyll radicalsElectron transferAlternate electron donorsEPR studiesEPR signalDistance estimatesReaction centersRadicalsSpectroscopy
2002
Structure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †
Vassiliev S, Lee C, Brudvig G, Bruce D. Structure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †. Biochemistry 2002, 41: 12236-12243. PMID: 12356326, DOI: 10.1021/bi0262597.Peer-Reviewed Original ResearchConceptsPSII core complexesFluorescence decay kineticsCharge separationRadical pairPhotosystem IIKinetic modelPhotosystem II core complexReaction centersFluorescence decayDecay kineticsII core complexesExcited-state dynamicsExcitation energy transferPrimary radical pairEnergy levelsStatic disorder modelElectron transferCharge stabilizationEnergy level modelExcited-state transferPSII preparationsStructure-based kinetic modelCore complexExponential decay componentsSimple kinetic model
2001
Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II
Vrettos J, Reifler M, Kievit O, Lakshmi K, de Paula J, Brudvig G. Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II. JBIC Journal Of Biological Inorganic Chemistry 2001, 6: 708-716. PMID: 11681704, DOI: 10.1007/s007750100249.Peer-Reviewed Original ResearchConceptsPCC 6803 photosystem IILow reduction potentialReduction potentialPyrolytic graphite edge electrodeElectron paramagnetic resonance spectroscopySquare wave voltammetryDirect electrochemical measurementsParamagnetic resonance spectroscopyBis-histidine axial ligationHeme reduction potentialCyanobacterial photosystem IIResonance Raman spectraPhotosystem IIWave voltammetryElectrode surfaceElectrochemistry experimentsElectrochemical measurementsElectrochemical valuesAxial ligationSolvent waterCyt c550Solvent exposureRedox titrationPeak separationPSII preparationsEffects of tail‐like substituents on the binding of competitive inhibitors to the QB site of photosystem II
Reifler M, Szalai V, Peterson C, Brudvig G. Effects of tail‐like substituents on the binding of competitive inhibitors to the QB site of photosystem II. Journal Of Molecular Recognition 2001, 14: 157-165. PMID: 11391786, DOI: 10.1002/jmr.529.Peer-Reviewed Original ResearchConceptsQB siteAqueous phasePhotosystem IIBulk aqueous phaseCritical micelle concentrationTriazine-type herbicidesQuinone-binding sitePhenylurea moietyEffect of chargeAlkyl chainsHydrophobic tailSolvent conditionsMicelle concentrationPara positionPhenylurea compoundsS-triazineAlkylamino groupSubstituentsSmall libraryHydrophobic linkerMolecular rulerHydrophilic domainsNonspecific bindingChargeCompetitive inhibitorCarotenoid 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
2000
Characterization of Carotenoid and Chlorophyll Photooxidation in Photosystem II †
Tracewell C, Cua A, Stewart D, Bocian D, Brudvig G. Characterization of Carotenoid and Chlorophyll Photooxidation in Photosystem II †. Biochemistry 2000, 40: 193-203. PMID: 11141071, DOI: 10.1021/bi001992o.Peer-Reviewed Original ResearchMeSH KeywordsCarotenoidsChlorophyllCyanobacteriaElectron Spin Resonance SpectroscopyFree RadicalsLight-Harvesting Protein ComplexesOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectroscopy, Near-InfraredSpectrum Analysis, RamanSpinacia oleraceaTemperatureThylakoidsConceptsSpinach PSII membranesPSII core complexesPSII membranesIR bandsElectron paramagnetic resonance spectroscopyAccessory chlorophyllPhotosystem IIParamagnetic resonance spectroscopyResonance Raman bandsPrevious spectroscopic studiesCation radicalsRaman difference spectroscopySpectroscopic studiesAlternate electron donorsElectron donorInfrared absorbanceCharacterization of carotenoidsRaman bandsResonance spectroscopyDifference spectroscopyHeme cofactorProtein conformersCore complexDifferent stabilitiesMultiphasic kineticsAssignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †
Stewart D, Nixon P, Diner B, Brudvig G. Assignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †. Biochemistry 2000, 39: 14583-14594. PMID: 11087414, DOI: 10.1021/bi001246j.Peer-Reviewed Original ResearchMeSH KeywordsBacteriochlorophyllsBenzoquinonesCold TemperatureCyanobacteriaElectron Spin Resonance SpectroscopyFree RadicalsFreezingGlutamineHistidineLight-Harvesting Protein ComplexesMutagenesis, Site-DirectedOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrophotometryTyrosineConceptsAbsorbance bandPhotosystem IIHydrogen bonding environmentOptical spectroscopyReaction center chromophoresRedox-active cofactorsDouble difference spectraLow temperature optical spectroscopyNumber of chromophoresRedox-active quinonesMutant reaction centersRedox stateRC chromophoresAxial ligandsCryogenic optical spectroscopyChromophore positionProtein environmentPSII preparationsSpectral assignmentsElectrochromic effectAccessory ChlElectronic structureChromophoreChromophore interactionsPhotosynthetic RCs
1999
Location of the Iron−Sulfur Clusters FA and FB in Photosystem I: An Electron Paramagnetic Resonance Study of Spin Relaxation Enhancement of P700 + †
Lakshmi K, Jung Y, Golbeck J, Brudvig G. Location of the Iron−Sulfur Clusters FA and FB in Photosystem I: An Electron Paramagnetic Resonance Study of Spin Relaxation Enhancement of P700 + †. Biochemistry 1999, 38: 13210-13215. PMID: 10529193, DOI: 10.1021/bi9910777.Peer-Reviewed Original Research
1998
Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †
Stewart D, Cua A, Chisholm D, Diner B, Bocian D, Brudvig G. Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †. Biochemistry 1998, 37: 10040-10046. PMID: 9665709, DOI: 10.1021/bi980668e.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonanceAxial ligandsChlorophyll ZPhotosystem IIRR spectraLow-temperature electron paramagnetic resonanceWild-type Photosystem IIRedox-active tyrosinesReaction centersEfficiency of photooxidationResonance Raman spectroscopyPSII complexesIR absorbance spectraD2 polypeptidesBacterial reaction centersParamagnetic resonanceRR signatureRaman spectroscopyAccessory ChlInfrared absorbanceQuantum yieldAbsorbance bandLigandsIR excitationLow-temperature illumination
1995
Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II.
Koulougliotis D, Tang X, Diner B, Brudvig G. Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II. Biochemistry 1995, 34: 2850-6. PMID: 7893698, DOI: 10.1021/bi00009a015.Peer-Reviewed Original Research
1993
Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center.
Tang X, Chisholm D, Dismukes G, Brudvig G, Diner B. Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center. Biochemistry 1993, 32: 13742-8. PMID: 8257709, DOI: 10.1021/bi00212a045.Peer-Reviewed Original Research
1991
A guide to electron paramagnetic resonance spectroscopy of Photosystem II membranes
Miller A, Brudvig G. A guide to electron paramagnetic resonance spectroscopy of Photosystem II membranes. Biochimica Et Biophysica Acta 1991, 1056: 1-18. PMID: 1845842, DOI: 10.1016/s0005-2728(05)80067-2.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyElectron paramagnetic resonance signalParamagnetic resonance spectroscopyParamagnetic resonance signalPhotosystem II membranesPhotosynthetic electron transportResonance spectroscopyResonance signalsPhotosystem IIBacterial reaction centersElectron transportParamagnetic speciesCytochrome b6fPhotosystem IBiochemical basisReaction centersSpectroscopySpeciesSpectral featuresCommon contaminantsMembraneMoietySeminal experimentsB6fCofactor
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