2017
Linker Length-Dependent Electron-Injection Dynamics of Trimesitylporphyrins on SnO2 Films
Lee S, Regan K, Hedström S, Matula A, Chaudhuri S, Crabtree R, Batista V, Schmuttenmaer C, Brudvig G. Linker Length-Dependent Electron-Injection Dynamics of Trimesitylporphyrins on SnO2 Films. The Journal Of Physical Chemistry C 2017, 121: 22690-22699. DOI: 10.1021/acs.jpcc.7b07855.Peer-Reviewed Original ResearchDye-sensitized photoelectrochemical cellsElectron injection dynamicsPhotoelectrochemical cellsLinker lengthMetal oxide filmsMolecular photosensitizersPorphyrin coreAnchor groupsElectron acceptorInjection dynamicsLinkerSnO2 filmsOxide filmsFilmsTerphenyleneSystematic studyPhenylenePorphyrinsBiphenyleneSpectroscopyComputational modelingAcceptorPhotosensitizerSynthesisOxide
2016
Surface-Induced Deprotection of THP-Protected Hydroxamic Acids on Titanium Dioxide
Brennan B, Koenigsmann C, Materna K, Kim P, Koepf M, Crabtree R, Schmuttenmaer C, Brudvig G. Surface-Induced Deprotection of THP-Protected Hydroxamic Acids on Titanium Dioxide. The Journal Of Physical Chemistry C 2016, 120: 12495-12502. DOI: 10.1021/acs.jpcc.6b02635.Peer-Reviewed Original ResearchDye-sensitized photoelectrochemical cellsMetal oxidesMetal oxide surfacesDirect surface functionalizationSurface-bound speciesConvenient new methodHydroxamic acidDye aggregationSurface speciesSurface functionalizationCovalent interactionsOxide surfaceHydroxamate groupHydrolytic stabilityPhotoelectrochemical cellsTiO2 surfaceStable complexesTitanium dioxideDeprotectionChelation methodBinding propertiesMK-2Room temperatureHydroxamateOxide
2010
Water -stable, hydroxamate anchors for functionalization of TiO 2 surfaces with ultrafast interfacial electron transfer
McNamara W, Milot R, Song H, Snoeberger R, Batista V, Schmuttenmaer C, Brudvig G, Crabtree R. Water -stable, hydroxamate anchors for functionalization of TiO 2 surfaces with ultrafast interfacial electron transfer. Energy & Environmental Science 2010, 3: 917-923. DOI: 10.1039/c001065k.Peer-Reviewed Original ResearchInterfacial electron transferUltrafast interfacial electron transferTiO2 nanoparticlesSolar energy conversionElectron transferPhotocatalytic cellsNanoparticlesOrganic dyesTiO 2 surfaceMetal oxidesEnergy conversionElectron injectionConduction bandTHz spectroscopyAqueous conditionsTiO2Transition metal complexesNeutral pHFunctionalizationMetal complexesCarboxylate anchorStrong bindingStable moleculesOxideCarboxylic acids
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
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
1980
Reactions of nitric oxide with cytochrome c oxidase.
Brudvig G, Stevens T, Chan S. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry 1980, 19: 5275-85. PMID: 6255988, DOI: 10.1021/bi00564a020.Peer-Reviewed Original Research