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
The X‐ray structure of photosystem II reveals a novel electron transport pathway between P680, cytochrome b 559 and the energy‐quenching cation, ChlZ +
Vasil’ev S, Brudvig G, Bruce D. The X‐ray structure of photosystem II reveals a novel electron transport pathway between P680, cytochrome b 559 and the energy‐quenching cation, ChlZ +. FEBS Letters 2003, 543: 159-163. PMID: 12753925, DOI: 10.1016/s0014-5793(03)00442-3.Peer-Reviewed Original Research
2002
Component 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 ResearchStructure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †
Vassiliev S, Lee C, Brudvig G, Bruce D. Structure-Based Kinetic Modeling of Excited-State Transfer and Trapping in Histidine-Tagged Photosystem II Core Complexes from Synechocystis †. Biochemistry 2002, 41: 12236-12243. PMID: 12356326, DOI: 10.1021/bi0262597.Peer-Reviewed Original ResearchConceptsPSII core complexesFluorescence decay kineticsCharge separationRadical pairPhotosystem IIKinetic modelPhotosystem II core complexReaction centersFluorescence decayDecay kineticsII core complexesExcited-state dynamicsExcitation energy transferPrimary radical pairEnergy levelsStatic disorder modelElectron transferCharge stabilizationEnergy level modelExcited-state transferPSII preparationsStructure-based kinetic modelCore complexExponential decay componentsSimple kinetic model
2001
Quantifying the Ion Selectivity of the Ca2+ Site in Photosystem II: Evidence for Direct Involvement of Ca2+ in O2 Formation †
Vrettos J, Stone D, Brudvig G. Quantifying the Ion Selectivity of the Ca2+ Site in Photosystem II: Evidence for Direct Involvement of Ca2+ in O2 Formation †. Biochemistry 2001, 40: 7937-7945. PMID: 11425322, DOI: 10.1021/bi010679z.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexTrivalent metal ionsMetal ionsPSII samplesPhotosystem IISubstrate water moleculesSmall metal ionsO2 evolutionSteady-state enzyme kineticsWater oxidationAqua ionsWater moleculesLewis acidO2 formationIonic radiusIon selectivityKcal/Monovalent ionsIonsExtrinsic polypeptidesFree energyEnzyme kineticsStructural cofactorSr2Activity measurementsMechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry
Vrettos J, Limburg J, Brudvig G. Mechanism of photosynthetic water oxidation: combining biophysical studies of photosystem II with inorganic model chemistry. Biochimica Et Biophysica Acta 2001, 1503: 229-245. PMID: 11115636, DOI: 10.1016/s0005-2728(00)00214-0.Peer-Reviewed Original ResearchMeSH KeywordsCrystallographyElectron TransportHemerythrinHydrogen-Ion ConcentrationKineticsManganeseModels, ChemicalModels, MolecularOrganometallic CompoundsOxidation-ReductionOxygenPhotosynthesisPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexProtonsThylakoidsTyrosineWaterConceptsPhotosynthetic water oxidationWater oxidationOxygen-evolving complexProton-coupled electron transferTetranuclear manganese clusterMu-oxo bridgePhotosystem IIReduction of manganeseOOH speciesWater moleculesElectron transferModel chemistryManganese clusterNucleophilic attackDiferric siteFerric hydroperoxideOxidationD1 polypeptideBiophysical studiesOxyhemerythrinBiophysical resultsStructural modelDioxygenChemistryProtonation
2000
Characterization of the O2-Evolving Reaction Catalyzed by [(terpy)(H2O)MnIII(O)2MnIV(OH2)(terpy)](NO3)3 (terpy = 2,2‘:6,2‘ ‘-Terpyridine)
Limburg J, Vrettos J, Chen H, de Paula J, Crabtree R, Brudvig G. Characterization of the O2-Evolving Reaction Catalyzed by [(terpy)(H2O)MnIII(O)2MnIV(OH2)(terpy)](NO3)3 (terpy = 2,2‘:6,2‘ ‘-Terpyridine). Journal Of The American Chemical Society 2000, 123: 423-430. PMID: 11456544, DOI: 10.1021/ja001090a.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 ConformationCharacterization of the Interaction between Manganese and Tyrosine Z in Acetate-Inhibited Photosystem II †
Szalai V, Kühne H, Lakshmi K, Brudvig G. Characterization of the Interaction between Manganese and Tyrosine Z in Acetate-Inhibited Photosystem II †. Biochemistry 1998, 37: 13594-13603. PMID: 9753446, DOI: 10.1021/bi9813025.Peer-Reviewed Original ResearchCalcium 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
Formation and Decay of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II †
Szalai V, Brudvig G. Formation and Decay of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II †. Biochemistry 1996, 35: 1946-1953. PMID: 8639678, DOI: 10.1021/bi952378t.Peer-Reviewed Original ResearchIsolation and Characterization of Spinach Photosystem II Membrane-Associated Catalase and Polyphenol Oxidase †
Sheptovitsky Y, Brudvig G. Isolation and Characterization of Spinach Photosystem II Membrane-Associated Catalase and Polyphenol Oxidase †. Biochemistry 1996, 35: 16255-16263. PMID: 8973199, DOI: 10.1021/bi9613842.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsCatalaseCatechol OxidaseChloroplastsChromatography, High Pressure LiquidChromatography, Ion ExchangeCopperElectrophoresis, Polyacrylamide GelHot TemperatureIntracellular MembranesKineticsMolecular WeightOxygenOxygen ConsumptionPeptide MappingPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrophotometrySpinacia oleraceaSubstrate SpecificityConceptsPSII membranesCentre of PSIIUV-visible absorptionO2 evolution activityThylakoid membranesSpinach thylakoid membranesAnion-exchange chromatographyMembrane-associated catalaseHeme enzymesBatch adsorptionHeme catalasesMild heat treatmentHeat treatmentMolecular weightAnion-exchange beadsNative molecular weightPPOIrreversible aggregationGel filtrationFurther manipulationAdsorptionAmino acid compositionTriazoleMembraneChromatography
1995
Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II.
Koulougliotis D, Tang X, Diner B, Brudvig G. Spectroscopic evidence for the symmetric location of tyrosines D and Z in photosystem II. Biochemistry 1995, 34: 2850-6. PMID: 7893698, DOI: 10.1021/bi00009a015.Peer-Reviewed Original Research[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
1992
Photooxidation of cytochrome b559 in oxygen-evolving photosystem II.
Buser C, Diner B, Brudvig G. Photooxidation of cytochrome b559 in oxygen-evolving photosystem II. Biochemistry 1992, 31: 11449-59. PMID: 1445880, DOI: 10.1021/bi00161a025.Peer-Reviewed Original ResearchConceptsCyt b559Photosystem II protein complexDark reductionOptical spectroscopyElectron transfer kineticsOxygen-evolving photosystem IIPSII-enriched membranesCytochrome b559Redox stateS2QA- charge recombinationExtent of photooxidationRate of photooxidationPrimary electron acceptorPH range 5.0Plastoquinone poolPSII samplesAcidic pH valuesRoom temperatureElectron acceptorPhotosystem IIPhotooxidationRate of reductionRedox equilibriumRange 5.0P680Using saturation-recovery EPR to measure distances in proteins: applications to photosystem II.
Hirsh D, Beck W, Innes J, Brudvig G. Using saturation-recovery EPR to measure distances in proteins: applications to photosystem II. Biochemistry 1992, 31: 532-41. PMID: 1310040, DOI: 10.1021/bi00117a033.Peer-Reviewed Original Research
1991
Mechanism of irreversible inhibition of O2 evolution in photosystem II by Tris(hydroxymethyl)aminomethane.
Rickert K, Sears J, Beck W, Brudvig G. Mechanism of irreversible inhibition of O2 evolution in photosystem II by Tris(hydroxymethyl)aminomethane. Biochemistry 1991, 30: 7888-94. PMID: 1651110, DOI: 10.1021/bi00246a003.Peer-Reviewed Original ResearchConceptsMn complexesPSII membranesRate of reactionO2 evolutionLow-temperature electron paramagnetic resonance (EPR) spectroscopyElectron paramagnetic resonance spectroscopyElectron donation reactionsPhotosystem IIElectron donation abilityParamagnetic resonance spectroscopyOxidation stateTris treatmentResonance spectroscopyS1 stateDark reactionTriIrreversible inhibitionReactionComplexesAminesIonsO2Effect of TrisMn2Spectroscopy
1990
Electron-transfer reactions in manganese-depleted photosystem II.
Buser C, Thompson L, Diner B, Brudvig G. Electron-transfer reactions in manganese-depleted photosystem II. Biochemistry 1990, 29: 8977-85. PMID: 2176840, DOI: 10.1021/bi00490a014.Peer-Reviewed Original ResearchConceptsMn-depleted photosystem II membranesElectron donation reactionsManganese-depleted photosystem IIElectron donationCytochrome b559Photosystem II membranesElectron paramagnetic resonance spectroscopyGlobal fitPSII samplesParamagnetic resonance spectroscopyEnergy differenceP680Room temperaturePhotosystem IIElectron transfer reactionsTime scalesLifetimeDecayFree energy differenceElectron transferRate constantsB559Resonance spectroscopySame orderRate of photooxidationElectron-transfer events leading to reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes.
Miller A, Brudvig G. Electron-transfer events leading to reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes. Biochemistry 1990, 29: 1385-92. PMID: 2159337, DOI: 10.1021/bi00458a007.Peer-Reviewed Original ResearchConceptsPhotooxidation of Mn2Photosystem II membranesO2 evolution activityMn complexesElectron donationMn-depleted photosystem IIPhotosystem IIElectron paramagnetic resonance spectroscopyFirst photochemical stepElectron donation reactionsCharge-separated stateElectron transfer eventsCytochrome bParamagnetic resonance spectroscopyMn-depleted photosystem II membranesOxygen evolution activityUntreated photosystem IILow quantum yieldSlower electron donationPhotochemical stepPrevious kinetic studiesTurnover reactionsElementary stepsElectron donorPhotooxidation
1989
Manganese and calcium requirements for reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes.
Miller A, Brudvig G. Manganese and calcium requirements for reconstitution of oxygen-evolution activity in manganese-depleted photosystem II membranes. Biochemistry 1989, 28: 8181-90. PMID: 2557898, DOI: 10.1021/bi00446a033.Peer-Reviewed Original Research