2024
Optical Pump THz Probe Spectroscopy on Metal-Organic Frameworks
Ostresh S, Nyakuchena J, Streater D, Wang D, Cody C, Hooper R, Zhang X, Reinhart B, Ma Q, He P, Brudvig G, Huang J, Neu J. Optical Pump THz Probe Spectroscopy on Metal-Organic Frameworks. 2024, fw4i.3. DOI: 10.1364/cleo_fs.2024.fw4i.3.Peer-Reviewed Original ResearchMetal-organic frameworksOptical pump-THz probePorous crystalline metal-organic frameworksCrystalline metal-organic frameworksCatalytic activity measurementsElectro-optical applicationsMetal centerProbe spectroscopyOptical pump-THz probe spectroscopyUltrafast photoconductivityPhotoconductivityTHz-probe spectroscopyPhotophysicsCatalysisChemical compositionTHz probeSpectroscopyMaterialsMetalChemical
2022
Highly stable preferential carbon monoxide oxidation by dinuclear heterogeneous catalysts
Zhao Y, Dai S, Yang K, Cao S, Materna K, Lant H, Kao L, Feng X, Guo J, Brudvig G, Flytzani-Stephanopoulos M, Batista V, Pan X, Wang D. Highly stable preferential carbon monoxide oxidation by dinuclear heterogeneous catalysts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 120: e2206850120. PMID: 36577066, PMCID: PMC9910598, DOI: 10.1073/pnas.2206850120.Peer-Reviewed Original ResearchRevealing the Structure of Single Cobalt Sites in Carbon Nitride for Photocatalytic CO2 Reduction
Huang P, Huang J, Li J, Pham T, Zhang L, He J, Brudvig G, Deskins N, Frenkel A, Li G. Revealing the Structure of Single Cobalt Sites in Carbon Nitride for Photocatalytic CO2 Reduction. The Journal Of Physical Chemistry C 2022, 126: 8596-8604. DOI: 10.1021/acs.jpcc.2c01216.Peer-Reviewed Original ResearchPhotocatalytic CO2 reductionSingle CO2CO2 reductionCarbon nitrideX-ray absorption spectroscopyCo-N bond lengthsImproved catalytic propertiesSingle Cobalt SitesMode of coordinationMore edge sitesGraphitic carbon nitrideObserved enhancement effectMetal centerCatalytic propertiesC3N4 materialsAbsorption spectroscopyBond lengthsSpectroscopic toolsPhotocatalytic propertiesExcellent activityCobalt sitesEdge sitesC3N4 flakesBinding energiesLight absorption
2013
3.15 Complex Systems: Photosynthesis
Pokhrel R, Brudvig G. 3.15 Complex Systems: Photosynthesis. 2013, 385-422. DOI: 10.1016/b978-0-08-097774-4.00313-2.Peer-Reviewed Original ResearchOxygen-evolving complexQuantum mechanics/molecular mechanicsPhotosystem IIOO bond formationDensity functional theory calculationsComplete catalytic cycleFunctional theory calculationsProton exit pathwayIron-sulfur centersMetal centerNatural photosynthesisModel complexesCatalytic cycleBond formationMolecular mechanicsFunctional mimicsElectronic characterizationTheory calculationsRole of chlorideOxygenic photosynthesisComplexesDetailed mechanismExit pathwayHydrogenasesPlastocyanin
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
1983
The metal centers of cytochrome c oxidase: Structure and function
Chan S, Blair D, Martin C, Wang H, Gelles J, Morgan J, Witt S, Birge R, Stevens T, Brudvig G. The metal centers of cytochrome c oxidase: Structure and function. Inorganica Chimica Acta 1983, 79: 72-73. DOI: 10.1016/s0020-1693(00)95101-6.Peer-Reviewed Original ResearchMetal centerTransmembrane electrochemical potential gradientDioxygen reductionElectron transferElectrochemical potential gradientDioxygen reduction reactionReduction of dioxygenUnambiguous structural informationProton pumpingEPR/ENDOR studyElectron transfer rate theoryOxygen reductionReduction reactionMetal sitesBiosynthetic procedureElectrochemical potential profilesFerryl intermediateENDOR studyReduction sitePotential gradientReaction originatesDioxygen reduction siteFree energyCytochrome c oxidaseStructural informationThe 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
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