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 6803
2002
Electronic Structure of the P700 Special Pair from High-Frequency Electron Paramagnetic Resonance Spectroscopy
Poluektov O, Utschig L, Schlesselman S, Lakshmi K, Brudvig G, Kothe G, Thurnauer M. Electronic Structure of the P700 Special Pair from High-Frequency Electron Paramagnetic Resonance Spectroscopy. The Journal Of Physical Chemistry B 2002, 106: 8911-8916. DOI: 10.1021/jp021465+.Peer-Reviewed Original ResearchElectron paramagnetic resonance spectroscopyParamagnetic resonance spectroscopyTriplet stateFrequency Electron Paramagnetic Resonance SpectroscopyElectronic structureHigh-frequency electron paramagnetic resonance spectroscopyResonance spectroscopyPrimary donorPrimary donor cationPhotosynthetic reaction centersHigh-frequency EPRDonor cationI. Electronic structureElectronic characterReaction centersValue anisotropySpecial pairTensor axesCationsSpectroscopyPhotosystem IP700T stateEPRStructure
2001
Electrochemical properties of [MnIII(terpy)(N3)3] (terpy=2,2′:6′,2″-terpyridine) in CH3CN Electrogeneration of dimanganese(II) di-μ-azido and dimanganese(IV) di-μ-oxo complexes
Baffert C, Chen H, Crabtree R, Brudvig G, Collomb M. Electrochemical properties of [MnIII(terpy)(N3)3] (terpy=2,2′:6′,2″-terpyridine) in CH3CN Electrogeneration of dimanganese(II) di-μ-azido and dimanganese(IV) di-μ-oxo complexes. Journal Of Electroanalytical Chemistry 2001, 506: 99-105. DOI: 10.1016/s0022-0728(01)00488-0.Peer-Reviewed Original ResearchQuasi-reversible reduction waveQuasi-reversible oxidation waveTetra-n-butylammonium perchlorateElectron paramagnetic resonance spectroscopyControlled-potential reductionOne-electron wavesDi-μ-azidoControlled-potential oxidationParamagnetic resonance spectroscopyExhaustive electrolysesM Bu4NClO4New mononuclearOxidation waveElectrochemical propertiesRedox coupleCH3CN solutionCyclic voltammogramsElectrochemical behaviorReduction waveAzide complexesReduced speciesQuantitative conversionOxidation processResonance spectroscopyResidual H2OUse of EPR Spectroscopy to Study Macromolecular Structure and Function
Biswas R, KÜhne H, Brudvig G, Gopalan V. Use of EPR Spectroscopy to Study Macromolecular Structure and Function. Science Progress 2001, 84: 45-68. PMID: 11382137, PMCID: PMC10367463, DOI: 10.3184/003685001783239050.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyProtein-nucleic acid complexesSpin-labeling reagentParamagnetic resonance spectroscopySpin labelsEPR spectroscopyAcid complexesBiological macromoleculesEPR spectraSite-specific substitutionMacromolecular structureResonance spectroscopyNucleic acidsSpectroscopyRecent applicationsStructural aspectsCommercial availabilityMacromoleculesCysteine residuesReagentsAdvent of techniquesStructure-function correlatesExperimental strategiesComplexesPowerful tool
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 kinetics
1996
EPR 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 bindingSemiquinone
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
1991
Mechanism of irreversible inhibition of O2 evolution in photosystem II by Tris(hydroxymethyl)aminomethane.
Rickert K, Sears J, Beck W, Brudvig G. Mechanism of irreversible inhibition of O2 evolution in photosystem II by Tris(hydroxymethyl)aminomethane. Biochemistry 1991, 30: 7888-94. PMID: 1651110, DOI: 10.1021/bi00246a003.Peer-Reviewed Original ResearchConceptsMn complexesPSII membranesRate of reactionO2 evolutionLow-temperature electron paramagnetic resonance (EPR) spectroscopyElectron paramagnetic resonance spectroscopyElectron donation reactionsPhotosystem IIElectron donation abilityParamagnetic resonance spectroscopyOxidation stateTris treatmentResonance spectroscopyS1 stateDark reactionTriIrreversible inhibitionReactionComplexesAminesIonsO2Effect of TrisMn2SpectroscopyA 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
1990
Electron-transfer reactions in manganese-depleted photosystem II.
Buser C, Thompson L, Diner B, Brudvig G. Electron-transfer reactions in manganese-depleted photosystem II. Biochemistry 1990, 29: 8977-85. PMID: 2176840, DOI: 10.1021/bi00490a014.Peer-Reviewed Original ResearchConceptsMn-depleted photosystem II membranesElectron donation reactionsManganese-depleted photosystem IIElectron donationCytochrome b559Photosystem II membranesElectron paramagnetic resonance spectroscopyGlobal fitPSII samplesParamagnetic resonance spectroscopyEnergy differenceP680Room temperaturePhotosystem IIElectron transfer reactionsTime scalesLifetimeDecayFree energy differenceElectron transferRate constantsB559Resonance spectroscopySame orderRate of photooxidation
1987
Reactions of hydroxylamine with the electron-donor side of photosystem II.
Beck W, Brudvig G. Reactions of hydroxylamine with the electron-donor side of photosystem II. Biochemistry 1987, 26: 8285-95. PMID: 2831941, DOI: 10.1021/bi00399a040.Peer-Reviewed Original ResearchConceptsReaction of hydroxylamineMn complexesElectron donor sideO2-evolving centerCharge separationPSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyPhotosystem IIElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalS1 stateTwo-electron reductionOne-electron photooxidationParamagnetic resonance spectroscopyN-methyl-substituted analoguesRadical oxidation productsO2 evolution activityMultiline EPR signalOxidation stateThylakoid membrane preparationsOxidation productsEvolution activityProlonged dark incubationEPR signalResonance spectroscopyFormation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide
Miller A, de Paula J, Brudvig G. Formation of the S2 state and structure of the Mn complex in photosystem II lacking the extrinsic 33 kilodalton polypeptide. Photosynthesis Research 1987, 12: 205-218. PMID: 24435688, DOI: 10.1007/bf00055121.Peer-Reviewed Original ResearchS2-state multiline EPR signalState multiline EPR signalStable charge separationPSII membranesMultiline EPR signalEPR signalCharge separationManganese sitesElectron paramagnetic resonance spectroscopyUntreated PSII membranesElectron transfer eventsParamagnetic resonance spectroscopyPhotosystem II membranesMn complexesElectron donorResonance spectroscopyS2 stateReaction centersExtrinsic polypeptidesHigh yieldsMagnetic propertiesPhotosystem IISeparationTemperature rangeSpectroscopy
1986
Binding of amines to the O2-evolving center of photosystem II.
Beck W, Brudvig G. Binding of amines to the O2-evolving center of photosystem II. Biochemistry 1986, 25: 6479-86. PMID: 3024709, DOI: 10.1021/bi00369a021.Peer-Reviewed Original ResearchConceptsO2-evolving centerMultiline EPR spectrumMultiline EPR signalEPR signalS2 statePSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyEPR spectraElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalPhotosystem IIBinding of NH3Untreated PSII membranesDirect spectroscopic evidenceParamagnetic resonance spectroscopySpinach PSII membranesMn sitesBinding of aminesDifferent EPR signalsNH3 moleculesSpectroscopic evidencePrimary aminesSteric factorsParamagnetic sitesResonance spectroscopy
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
1983
The Structure of the Metal Centers in Cytochrome c Oxidase
Chan S, Martin C, Wang H, Brudvig G, Stevens T. The Structure of the Metal Centers in Cytochrome c Oxidase. Nato Science Series C: 1983, 313-328. DOI: 10.1007/978-94-009-7049-6_27.Peer-Reviewed Original ResearchMetal centerLow-temperature electron paramagnetic resonance (EPR) spectroscopyElectron nuclear double resonance spectroscopyNuclear double resonance spectroscopyElectron paramagnetic resonance spectroscopyResonance spectroscopyParamagnetic resonance spectroscopyLow-temperature EPRO2 reduction siteDouble resonance spectroscopyReduction siteSpectroscopyCytochrome c oxidaseC oxidaseUnambiguous informationStructureEPRAmino acidsOxidaseOxideElucidationAcidNitric oxide