2011
Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II
Pokhrel R, McConnell IL, Brudvig GW. Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II. Biochemistry 2011, 50: 2725-2734. PMID: 21366335, DOI: 10.1021/bi2000388.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexPhotosystem IICatalytic residuesChloride-binding siteRecent structural evidenceCyanobacterial photosystem IISalt bridgeEnzyme-substrate complexΑ-amylaseResidue crucialConformational shiftS-state cycleLys residuesCarboxylate residuesEnzyme turnoverChloride regulationResiduesD61Structural evidenceManganese clusterEnzymeBindingD1Potential mechanismsArg
2006
Molecular Recognition in the Selective Oxygenation of Saturated C-H Bonds by a Dimanganese Catalyst
Das S, Incarvito CD, Crabtree RH, Brudvig GW. Molecular Recognition in the Selective Oxygenation of Saturated C-H Bonds by a Dimanganese Catalyst. Science 2006, 312: 1941-1943. PMID: 16809537, DOI: 10.1126/science.1127899.Peer-Reviewed Original ResearchConceptsHydrogen bondingMolecular recognitionH bondsCarboxylic acid groupsMolecular recognition elementsSynthetic catalystsSaturated CKemp's triacidSelective oxygenationCOOH groupRegioselective functionalizationH activationHigh selectivityAcid groupsRecognition groupReactive centerRecognition elementCatalystTriacidOrient substratesSelectivityBondingBondsControl experimentsSubstrate
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
2002
Water oxidation chemistry of photosystem II
Vrettos J, Brudvig G. Water oxidation chemistry of photosystem II. Philosophical Transactions Of The Royal Society B Biological Sciences 2002, 357: 1395-1405. PMID: 12437878, PMCID: PMC1693042, DOI: 10.1098/rstb.2002.1136.Peer-Reviewed Original ResearchConceptsManganese clusterProton-coupled electron transfer stepsO bond-forming stepPhotosystem IIWater oxidation chemistryBond-forming stepElectron transfer stepFour-electron oxidationTetranuclear manganese clusterOxidation chemistryWater moleculesModel chemistryO bondNucleophilic attackIon selectivityBiophysical studiesChemistryCalcium sitesOxidationSpecific roleModel systemComplexesHis190Recent studiesWaterComponent B Binding to the Soluble Methane Monooxygenase Hydroxylase by Saturation-Recovery EPR Spectroscopy of Spin-Labeled MMOB
MacArthur R, Sazinsky M, Kühne H, Whittington D, Lippard S, Brudvig G. Component B Binding to the Soluble Methane Monooxygenase Hydroxylase by Saturation-Recovery EPR Spectroscopy of Spin-Labeled MMOB. Journal Of The American Chemical Society 2002, 124: 13392-13393. PMID: 12418885, DOI: 10.1021/ja0279904.Peer-Reviewed Original Research
1999
Competitive Binding of Acetate and Chloride in Photosystem II †
Kühne H, Szalai V, Brudvig G. Competitive Binding of Acetate and Chloride in Photosystem II †. Biochemistry 1999, 38: 6604-6613. PMID: 10350479, DOI: 10.1021/bi990341t.Peer-Reviewed Original ResearchMapping RNA−Protein Interactions in Ribonuclease P from Escherichia coli Using Electron Paramagnetic Resonance Spectroscopy †
Gopalan V, Kühne H, Biswas R, Li H, Brudvig G, Altman S. Mapping RNA−Protein Interactions in Ribonuclease P from Escherichia coli Using Electron Paramagnetic Resonance Spectroscopy †. Biochemistry 1999, 38: 1705-1714. PMID: 10026248, DOI: 10.1021/bi9807106.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBinding SitesComputer SimulationElectron Spin Resonance SpectroscopyEndoribonucleasesEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein FoldingRibonuclease PRibonucleoproteinsRNA, BacterialRNA, CatalyticSpin LabelsStructure-Activity RelationshipConceptsM1 RNAC5 proteinRibonuclease PCysteine residuesEscherichia coliRNA-protein interfaceCatalytic RNA subunitNative cysteine residuesSulfhydryl-specific reagentsCatalytic ribonucleoproteinRNA subunitHoloenzyme complexRNP complexesProtein cofactorsMutant derivativesDeletion derivativesRNASpin labelsProteinSpectroscopy-based approachRibonucleoproteinResiduesPosition 16Coli
1998
Calcium Binding Studies of Photosystem II Using a Calcium-Selective Electrode †
Grove G, Brudvig G. Calcium Binding Studies of Photosystem II Using a Calcium-Selective Electrode †. Biochemistry 1998, 37: 1532-1539. PMID: 9484223, DOI: 10.1021/bi971356z.Peer-Reviewed Original Research
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
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 ResearchMeSH KeywordsBinding SitesElectron Transport Complex IVNitric OxideOxidation-ReductionOxygenProtein BindingSpectrum Analysis