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
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
2001
Pulsed electron paramagnetic resonance methods for macromolecular structure determination
Lakshmi K, Brudvig G. Pulsed electron paramagnetic resonance methods for macromolecular structure determination. Current Opinion In Structural Biology 2001, 11: 523-531. PMID: 11785751, DOI: 10.1016/s0959-440x(00)00242-6.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance methodHigh-field EPRParamagnetic resonance methodMacromolecular structure determinationStructure elucidationEPR distance measurementsMacromolecular systemsStructure determinationStructure/function relationshipsRecent applicationsResonance methodMicrowave technologyFunction relationshipsEPRDeterminationRecent developmentsReview articlePowerful toolElucidationPhotosynthetic Water Oxidation in Cytochromeb 559 Mutants Containing a Disrupted Heme-binding Pocket*
Morais F, Kühn K, Stewart D, Barber J, Brudvig G, Nixon P. Photosynthetic Water Oxidation in Cytochromeb 559 Mutants Containing a Disrupted Heme-binding Pocket*. Journal Of Biological Chemistry 2001, 276: 31986-31993. PMID: 11390403, DOI: 10.1074/jbc.m103935200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCarrier ProteinsChlamydomonas reinhardtiiCytochrome b GroupDNA PrimersElectron Spin Resonance SpectroscopyHeme-Binding ProteinsHemeproteinsMutagenesis, Site-DirectedMutationOxidation-ReductionPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexWaterConceptsPhotosynthetic oxygen evolutionMethionine mutantsWild typeAlpha subunitLight-saturated ratePhotosystem two complexWild-type levelsHeme of cytochromePhotosynthetic water oxidationHeme-binding pocketOxygen evolutionChloroplast mutantsPSII supercomplexesHistidine axial ligandsChlamydomonas reinhardtiiGlutamine mutantTyrosine mutantsMutantsType levelsRedox roleHemeSubunitsOxygen evolution activityTyrosineComplexesUse of EPR Spectroscopy to Study Macromolecular Structure and Function
Biswas R, KÜhne H, Brudvig G, Gopalan V. Use of EPR Spectroscopy to Study Macromolecular Structure and Function. Science Progress 2001, 84: 45-68. PMID: 11382137, PMCID: PMC10367463, DOI: 10.3184/003685001783239050.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyProtein-nucleic acid complexesSpin-labeling reagentParamagnetic resonance spectroscopySpin labelsEPR spectroscopyAcid complexesBiological macromoleculesEPR spectraSite-specific substitutionMacromolecular structureResonance spectroscopyNucleic acidsSpectroscopyRecent applicationsStructural aspectsCommercial availabilityMacromoleculesCysteine residuesReagentsAdvent of techniquesStructure-function correlatesExperimental strategiesComplexesPowerful tool
1996
Characterization of the Reductase Domain of Rat Neuronal Nitric Oxide Synthase Generated in the Methylotrophic Yeast Pichia pastoris CALMODULIN RESPONSE IS COMPLETE WITHIN THE REDUCTASE DOMAIN ITSELF*
Gachhui R, Presta A, Bentley D, Abu-Soud H, McArthur R, Brudvig G, Ghosh D, Stuehr D. Characterization of the Reductase Domain of Rat Neuronal Nitric Oxide Synthase Generated in the Methylotrophic Yeast Pichia pastoris CALMODULIN RESPONSE IS COMPLETE WITHIN THE REDUCTASE DOMAIN ITSELF*. Journal Of Biological Chemistry 1996, 271: 20594-20602. PMID: 8702805, DOI: 10.1074/jbc.271.34.20594.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCalmodulinCalmodulin-Binding ProteinsDNA PrimersElectron Spin Resonance SpectroscopyFlavinsFlavoproteinsIsoenzymesMolecular Sequence DataNADH DehydrogenaseNeuronsNitric Oxide SynthaseOxidation-ReductionPichiaRatsRecombinant ProteinsSpectrometry, FluorescenceTryptophanConceptsElectron transferFlavin semiquinoneReductase domainNADPH-dependent flavin reductionArtificial electron acceptorsADP affinity chromatographyHeme-containing oxygenase domainCalmodulin responseNNOS reductase domainAnaerobic titrationFlavin reductionElectron acceptorNNOS reductaseFlavin-containing reductase domainReductase proteinSemiquinoneFlavinFlavin fluorescenceOxygenase domainAffinity chromatographyCytochrome c.Pure proteinCytochrome cTransferAcceptorEPR 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
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
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
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
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
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 ResearchCua3 of cytochrome c oxidase is not a type 1 (blue) copper
Brudvig G, Chan S. Cua3 of cytochrome c oxidase is not a type 1 (blue) copper. FEBS Letters 1979, 106: 139-141. PMID: 227722, DOI: 10.1016/0014-5793(79)80712-7.Peer-Reviewed Original ResearchStructure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies.
Stevens T, Brudvig G, Bocian D, Chan S. Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies. Proceedings Of The National Academy Of Sciences Of The United States Of America 1979, 76: 3320-3324. PMID: 226967, PMCID: PMC383817, DOI: 10.1073/pnas.76.7.3320.Peer-Reviewed Original Research