2004
The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain*
Konas D, Zhu K, Sharma M, Aulak K, Brudvig G, Stuehr D. The FAD-shielding Residue Phe1395 Regulates Neuronal Nitric-oxide Synthase Catalysis by Controlling NADP+ Affinity and a Conformational Equilibrium within the Flavoprotein Domain*. Journal Of Biological Chemistry 2004, 279: 35412-35425. PMID: 15180983, DOI: 10.1074/jbc.m400872200.Peer-Reviewed Original Research
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
1998
Cytochrome b559 of photosystem II
Stewart D, Brudvig G. Cytochrome b559 of photosystem II. Biochimica Et Biophysica Acta 1998, 1367: 63-87. PMID: 9784607, DOI: 10.1016/s0005-2728(98)00139-x.Peer-Reviewed Original ResearchAmino Acid SequenceChemical PhenomenaChemistry, PhysicalCytochrome b GroupElectron TransportKineticsModels, BiologicalModels, MolecularMolecular Sequence DataOxidation-ReductionPhotochemistryPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtein Conformation
1995
[22] Electron paramagnetic resonance spectroscopy
Brudvig G. [22] Electron paramagnetic resonance spectroscopy. Methods In Enzymology 1995, 246: 536-554. PMID: 7752937, DOI: 10.1016/0076-6879(95)46024-1.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyParamagnetic resonance spectroscopyX-band EPR spectrometerEPR spectroscopyParamagnetic speciesResonance spectroscopyParamagnetic centersBiological systemsEPR spectrometerRedox reactionsDiamagnetic proteinsEPR spectraActive siteEPR methodSpectroscopySample requirementsSpectrometerEPRReactionValuable techniqueSpectraApplicationsSpeciesStructure
1989
Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II.
Innes J, Brudvig G. Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II. Biochemistry 1989, 28: 1116-25. PMID: 2540815, DOI: 10.1021/bi00429a028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsChlorophyllElectron Spin Resonance SpectroscopyFree RadicalsKineticsLight-Harvesting Protein ComplexesMathematicsMicrowavesModels, MolecularModels, TheoreticalMyoglobinPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsProtein ConformationRhodobacter sphaeroidesThermodynamicsTyrosineWhalesConceptsMetal ionsPSII membranesPhotosystem IIProtein surfaceMicrowave power saturationReaction centersRaman relaxation mechanismMagnetic relaxation propertiesFree radicalsRelaxation enhancementDipolar relaxation enhancementIonsMembrane surfaceRelaxation propertiesSpin-lattice relaxationComplexesDipolar interactionsRadicalsRhodobacter sphaeroidesProtein structureD2 subunitsPower saturationDy3Relaxation mechanismSurface
1981
Conformations of oxidized cytochrome c oxidase.
Brudvig G, Stevens T, Morse R, Chan S. Conformations of oxidized cytochrome c oxidase. Biochemistry 1981, 20: 3912-21. PMID: 6268153, DOI: 10.1021/bi00516a039.Peer-Reviewed Original Research
1979
Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region.
Bocian D, Lemley A, Petersen N, Brudvig G, Chan S. Resonance Raman spectra of cytochrome c oxidase. Excitation in the 600-nm region. Biochemistry 1979, 18: 4396-402. PMID: 226125, DOI: 10.1021/bi00587a020.Peer-Reviewed Original Research