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 6803Pulsed 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
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
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
Characterization of the Interaction between Manganese and Tyrosine Z in Acetate-Inhibited Photosystem II †
Szalai V, Kühne H, Lakshmi K, Brudvig G. Characterization of the Interaction between Manganese and Tyrosine Z in Acetate-Inhibited Photosystem II †. Biochemistry 1998, 37: 13594-13603. PMID: 9753446, DOI: 10.1021/bi9813025.Peer-Reviewed Original Research
1996
Effects of Dipole–Dipole Interactions on Microwave Progressive Power Saturation of Radicals in Proteins
Galli C, Innes J, Hirsh D, Brudvig G. Effects of Dipole–Dipole Interactions on Microwave Progressive Power Saturation of Radicals in Proteins. Journal Of Magnetic Resonance 1996, 110: 284-287. PMID: 8867444, DOI: 10.1006/jmrb.1996.0044.Peer-Reviewed Original ResearchEPR Spectroscopic Characterization of Neuronal NO Synthase †
Galli C, MacArthur R, Abu-Soud H, Clark P, Stuehr D, Brudvig G. EPR Spectroscopic Characterization of Neuronal NO Synthase †. Biochemistry 1996, 35: 2804-2810. PMID: 8611587, DOI: 10.1021/bi9520444.Peer-Reviewed Original ResearchConceptsSpin-spin couplingElectron transferHeme ironElectron paramagnetic resonance spectroscopyEPR spectroscopic characterizationParamagnetic resonance spectroscopyOxygenase domainZero-field splitting parametersFirst coordination shellHeme redox centersNNOS oxygenase domainAir-stable semiquinoneSpectroscopic characterizationRedox centersReductase domainFlavin radicalsInterdomain electron transferFlavin semiquinoneCoordination shellResonance spectroscopyMicrowave power saturationSubstrates bindAnaerobic conditionsSubstrate bindingSemiquinoneFormation and Decay of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II †
Szalai V, Brudvig G. Formation and Decay of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II †. Biochemistry 1996, 35: 1946-1953. PMID: 8639678, DOI: 10.1021/bi952378t.Peer-Reviewed Original Research
1995
[22] Electron paramagnetic resonance spectroscopy
Brudvig G. [22] Electron paramagnetic resonance spectroscopy. Methods In Enzymology 1995, 246: 536-554. PMID: 7752937, DOI: 10.1016/0076-6879(95)46024-1.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyParamagnetic resonance spectroscopyX-band EPR spectrometerEPR spectroscopyParamagnetic speciesResonance spectroscopyParamagnetic centersBiological systemsEPR spectrometerRedox reactionsDiamagnetic proteinsEPR spectraActive siteEPR methodSpectroscopySample requirementsSpectrometerEPRReactionValuable techniqueSpectraApplicationsSpeciesStructure
1992
Reevaluation of the stoichiometry of cytochrome b559 in photosystem II and thylakoid membranes.
Buser C, Diner B, Brudvig G. Reevaluation of the stoichiometry of cytochrome b559 in photosystem II and thylakoid membranes. Biochemistry 1992, 31: 11441-8. PMID: 1332760, DOI: 10.1021/bi00161a024.Peer-Reviewed Original Research
1989
Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II.
Innes J, Brudvig G. Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II. Biochemistry 1989, 28: 1116-25. PMID: 2540815, DOI: 10.1021/bi00429a028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsChlorophyllElectron Spin Resonance SpectroscopyFree RadicalsKineticsLight-Harvesting Protein ComplexesMathematicsMicrowavesModels, MolecularModels, TheoreticalMyoglobinPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsProtein ConformationRhodobacter sphaeroidesThermodynamicsTyrosineWhalesConceptsMetal ionsPSII membranesPhotosystem IIProtein surfaceMicrowave power saturationReaction centersRaman relaxation mechanismMagnetic relaxation propertiesFree radicalsRelaxation enhancementDipolar relaxation enhancementIonsMembrane surfaceRelaxation propertiesSpin-lattice relaxationComplexesDipolar interactionsRadicalsRhodobacter sphaeroidesProtein structureD2 subunitsPower saturationDy3Relaxation mechanismSurface
1984
Electron spin relaxation of CuA and cytochrome a in cytochrome c oxidase. Comparison to heme, copper, and sulfur radical complexes.
Brudvig G, Blair D, Chan S. Electron spin relaxation of CuA and cytochrome a in cytochrome c oxidase. Comparison to heme, copper, and sulfur radical complexes. Journal Of Biological Chemistry 1984, 259: 11001-11009. PMID: 6088526, DOI: 10.1016/s0021-9258(18)90613-7.Peer-Reviewed Original ResearchConceptsType 1 copperType 2 copperSulfur radicalsBlue copper proteinsMetal centerCopper complexesRadical complexesCopper centerCO complexCopper proteinsProtein environmentLow-spin heme proteinsParamagnetic sitesSpin centersHeme proteinsInorganic copperMagnetic dipolar interactionElectron spin relaxationCopperComplexesSpin-lattice relaxationDipolar interactionsCytochrome c oxidaseRadicalsCuA