2007
Ultrafast Photooxidation of Mn(II)−Terpyridine Complexes Covalently Attached to TiO2 Nanoparticles
Abuabara S, Cady C, Baxter J, Schmuttenmaer C, Crabtree R, Brudvig G, Batista V. Ultrafast Photooxidation of Mn(II)−Terpyridine Complexes Covalently Attached to TiO2 Nanoparticles. The Journal Of Physical Chemistry C 2007, 111: 11982-11990. DOI: 10.1021/jp072380h.Peer-Reviewed Original ResearchInterfacial electron transferTiO2 nanoparticlesColloidal thin filmsVisible light sensitizationElectron transferTime-resolved measurementsSurface modificationNanoparticlesThin filmsTiO2 surfaceAqueous suspensionTransient measurementsEPR signalPhotoexcitationMeasurementsComputational simulationsFilmsFSSpectroscopyComplexesPhotooxidationTransferSurfaceSignals
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 stateStateDoubletSpectraSignalsGHzLocation of EPR-Active Spins Buried in Proteins from the Simulation of the Spin−Lattice Relaxation Enhancement Caused by Dy(III) Complexes †
MacArthur R, Brudvig G. Location of EPR-Active Spins Buried in Proteins from the Simulation of the Spin−Lattice Relaxation Enhancement Caused by Dy(III) Complexes †. The Journal Of Physical Chemistry B 2004, 108: 9390-9396. DOI: 10.1021/jp0355713.Peer-Reviewed Original ResearchRelaxation enhancement agentsPower saturation characteristicsIndividual moleculesRadical spinsPower saturation experimentsFrozen solutionsRelaxation enhancementEPR signalSeries of spectraProtein moleculesProtein samplesProtein solutionsStructural dataMoleculesFree radicalsHorseradish peroxidaseRelaxation rateComputational methods
2003
Pulsed 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
1998
A Structural and Mechanistic Model of the O2-Evolving Complex of Photosystem II
Szalai V, Stone D, Brudvig G. A Structural and Mechanistic Model of the O2-Evolving Complex of Photosystem II. 1998, 1403-1406. DOI: 10.1007/978-94-011-3953-3_331.Peer-Reviewed Original ResearchElectron paramagnetic resonanceMn4 clusterO bond-forming stepReactivity of MnBond-forming stepWater oxidation siteWater/hydroxidePhotosystem II membranesPoint-dipole approximationMN4 complexesElectron transferO speciesParamagnetic resonanceEPR signalS2 stateSpectral simulationsPhotosystem IIYZComplexesMn atomsStructural modelCluster orientationChemistryHydroxideAtoms
1996
Reversible Binding of Nitric Oxide to Tyrosyl Radicals in Photosystem II. Nitric Oxide Quenches Formation of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II†
Szalai V, Brudvig G. Reversible Binding of Nitric Oxide to Tyrosyl Radicals in Photosystem II. Nitric Oxide Quenches Formation of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II†. Biochemistry 1996, 35: 15080-15087. PMID: 8942675, DOI: 10.1021/bi961117w.Peer-Reviewed Original ResearchConceptsS3 EPR signalOxygen-evolving complexMultiline EPR signalEPR signalS2 statePhotosystem IIManganese-depleted photosystem IIS2-state multiline EPR signalRedox-active tyrosinesPhotosystem II samplesRadical EPR signalSignal speciesNitric oxide (NO) bindsTyrosyl radicalsAmmonia resultsReversible bindingOxideYZDipolar interactionsRibonucleotide reductase
1989
Characterization of the multiple forms of cytochrome b559 in photosystem II.
Thompson L, Miller A, Buser C, de Paula J, Brudvig G. Characterization of the multiple forms of cytochrome b559 in photosystem II. Biochemistry 1989, 28: 8048-56. PMID: 2557895, DOI: 10.1021/bi00446a012.Peer-Reviewed Original ResearchConceptsCytochrome b559PSII membranesPhotosystem II protein complexUntreated PSII membranesExtrinsic polypeptidesLow-temperature photooxidationMn complexesPSII samplesEPR spectroscopyLigand fieldRedox titrationRedox formsEPR signalPhotosystem IIB559ComplexesThylakoid membranesPhotooxidationSpectroscopyProtein complexesUnique abilityMembraneTitrationConformationRemoval
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 spectroscopyEffect of the 17- and 23-kilodalton polypeptides, calcium, and chloride on electron transfer in photosystem II.
De Paula J, Li P, Miller A, Wu B, Brudvig G. Effect of the 17- and 23-kilodalton polypeptides, calcium, and chloride on electron transfer in photosystem II. Biochemistry 1986, 25: 6487-94. PMID: 3024710, DOI: 10.1021/bi00369a022.Peer-Reviewed Original ResearchConceptsS2-state multiline EPR signalMultiline EPR signalEPR signalPSII membranesPhotosystem II samplesS1 stateUntreated PSII membranesReaction centersElectron paramagnetic resonance measurementsChlorophyll moleculesPhotosystem II membranesStable charge separationParamagnetic resonance measurementsPhotosystem IIPSII samplesO2-evolving centerElectron transferCharge separationElectron donorNuclear hyperfine structureCytochrome b559Mn sitesResonance measurementsOxidationFraction of PSII
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
PROPERTIES OF THE S2 STATE ASSOCIATED WITH O2 EVOLUTION
Brudvig G, Casey J, Sauer K. PROPERTIES OF THE S2 STATE ASSOCIATED WITH O2 EVOLUTION. 1983, 159-164. DOI: 10.1016/b978-0-12-372360-4.50023-7.Peer-Reviewed Original ResearchS2 stateMultiline electron paramagnetic resonance (EPR) signalParamagnetic speciesO2 evolutionOxidation state changesPhotosynthetic water oxidationFinal oxidation productsElectron paramagnetic resonance signalS2 state EPR signalsCharge separation eventsS-state advancementMolecule of O2State EPR signalsParamagnetic resonance signalO2-evolving complexWater oxidationPhotosystem IIUnpaired electronOxidation productsEPR signalHyperfine structureResonance signalsSpinach chloroplastsSpeciesHyperfine lines