2015
Interfacial electron transfer in photoanodes based on phosphorus( v ) porphyrin sensitizers co-deposited on SnO 2 with the Ir(III)Cp* water oxidation precatalyst
Poddutoori P, Thomsen J, Milot R, Sheehan S, Negre C, Garapati V, Schmuttenmaer C, Batista V, Brudvig G, van der Est A. Interfacial electron transfer in photoanodes based on phosphorus( v ) porphyrin sensitizers co-deposited on SnO 2 with the Ir(III)Cp* water oxidation precatalyst. Journal Of Materials Chemistry A 2015, 3: 3868-3879. DOI: 10.1039/c4ta07018f.Peer-Reviewed Original ResearchInterfacial electron transferElectron paramagnetic resonanceQuantum dynamics simulationsElectron transferPhotoanode componentCatalytic water oxidationEfficient interfacial electron transferDynamics simulationsMetal oxide surfacesSolar cellsTime-resolved terahertz spectroscopy measurementsSteady-state fluorescenceTypes of porphyrinsTerahertz spectroscopy measurementsOxidation precatalystWater oxidationAxial coordinationChloride ligandsPorphyrin sensitizersOxidation stateCharge recombinationParamagnetic resonanceSnO 2Phosphorus porphyrinsSpectroscopy measurements
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 illuminationA 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
1988
Electron Donation in Photosystem II
Thompson L, Miller A, De Paula J, Brudvig G. Electron Donation in Photosystem II. Israel Journal Of Chemistry 1988, 28: 121-128. DOI: 10.1002/ijch.198800021.Peer-Reviewed Original ResearchElectron transfer pathwayElectron paramagnetic resonanceElectron donationTransfer pathwayElectron donorOxygen-evolving centerPS IIOptical spectroscopyPhotosystem IITime-resolved optical spectroscopyPrimary electron donorAlternate electron donorsParamagnetic resonanceEPR resultsCytochrome b 559EPR studiesCyclic electron transfer pathwaysMn sitesSpectroscopyPhotooxidationKinetic componentsPhotooxidation of chlorophyllDonorsKinetics
1982
The nature of CuA in cytochrome c oxidase.
Stevens T, Martin C, Wang H, Brudvig G, Scholes C, Chan S. The nature of CuA in cytochrome c oxidase. Journal Of Biological Chemistry 1982, 257: 12106-12113. PMID: 6288707, DOI: 10.1016/s0021-9258(18)33685-8.Peer-Reviewed Original ResearchConceptsCytochrome c oxidaseYeast cytochrome c oxidaseC oxidaseCysteine sulfurProteinBeef heartOxidaseElectron nuclear double resonance (ENDOR) spectraElectron paramagnetic resonanceSubstantial spin densityParamagnetic resonanceDouble resonance spectraBetaCuAResonance spectraCysteineSpin densityHistidine
1980
Evidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation
Brudvig G, Bocian D, Gamble R, Chan S. Evidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation. Biochimica Et Biophysica Acta 1980, 624: 78-89. PMID: 6250634, DOI: 10.1016/0005-2795(80)90227-5.Peer-Reviewed Original ResearchConceptsConventional X-ray sourceStanford Synchrotron Radiation LaboratoryX-ray absorption measurementsX-ray photonsPhotons/sX-ray fluxX-ray sourcesSynchrotron Radiation LaboratoryMetal centerOptical spectroscopyRadiation LaboratoryAbsorption measurementsElectron paramagnetic resonanceParamagnetic resonanceCytochrome c oxidasePhotonsPhotoreductionC oxidaseRadiationResonanceSpectroscopyOxidaseSourceMeasurementsFlux