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
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 studiesWater
2001
Mechanism 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
1999
Location of the Iron−Sulfur Clusters FA and FB in Photosystem I: An Electron Paramagnetic Resonance Study of Spin Relaxation Enhancement of P700 + †
Lakshmi K, Jung Y, Golbeck J, Brudvig G. Location of the Iron−Sulfur Clusters FA and FB in Photosystem I: An Electron Paramagnetic Resonance Study of Spin Relaxation Enhancement of P700 + †. Biochemistry 1999, 38: 13210-13215. PMID: 10529193, DOI: 10.1021/bi9910777.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
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
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
1991
A guide to electron paramagnetic resonance spectroscopy of Photosystem II membranes
Miller A, Brudvig G. A guide to electron paramagnetic resonance spectroscopy of Photosystem II membranes. Biochimica Et Biophysica Acta 1991, 1056: 1-18. PMID: 1845842, DOI: 10.1016/s0005-2728(05)80067-2.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonance spectroscopyElectron paramagnetic resonance signalParamagnetic resonance spectroscopyParamagnetic resonance signalPhotosystem II membranesPhotosynthetic electron transportResonance spectroscopyResonance signalsPhotosystem IIBacterial reaction centersElectron transportParamagnetic speciesCytochrome b6fPhotosystem IBiochemical basisReaction centersSpectroscopySpeciesSpectral featuresCommon contaminantsMembraneMoietySeminal experimentsB6fCofactor
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
Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680.
Metz J, Nixon P, Rögner M, Brudvig G, Diner B. Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680. Biochemistry 1989, 28: 6960-9. PMID: 2510819, DOI: 10.1021/bi00443a028.Peer-Reviewed Original Research
1988
Cytochrome b-559 may function to protect photosystem II from photoinhibition.
Thompson L, Brudvig G. Cytochrome b-559 may function to protect photosystem II from photoinhibition. Biochemistry 1988, 27: 6653-8. PMID: 3058202, DOI: 10.1021/bi00418a002.Peer-Reviewed Original Research
1987
Reactions of hydroxylamine with the electron-donor side of photosystem II.
Beck W, Brudvig G. Reactions of hydroxylamine with the electron-donor side of photosystem II. Biochemistry 1987, 26: 8285-95. PMID: 2831941, DOI: 10.1021/bi00399a040.Peer-Reviewed Original ResearchConceptsReaction of hydroxylamineMn complexesElectron donor sideO2-evolving centerCharge separationPSII membranesLow-temperature electron paramagnetic resonance (EPR) spectroscopyPhotosystem IIElectron paramagnetic resonance spectroscopyS2-state multiline EPR signalS1 stateTwo-electron reductionOne-electron photooxidationParamagnetic resonance spectroscopyN-methyl-substituted analoguesRadical oxidation productsO2 evolution activityMultiline EPR signalOxidation stateThylakoid membrane preparationsOxidation productsEvolution activityProlonged dark incubationEPR signalResonance spectroscopy
1986
Effect of the 17- and 23-kilodalton polypeptides, calcium, and chloride on electron transfer in photosystem II.
De Paula J, Li P, Miller A, Wu B, Brudvig G. Effect of the 17- and 23-kilodalton polypeptides, calcium, and chloride on electron transfer in photosystem II. Biochemistry 1986, 25: 6487-94. PMID: 3024710, DOI: 10.1021/bi00369a022.Peer-Reviewed Original ResearchConceptsS2-state multiline EPR signalMultiline EPR signalEPR signalPSII membranesPhotosystem II samplesS1 stateUntreated PSII membranesReaction centersElectron paramagnetic resonance measurementsChlorophyll moleculesPhotosystem II membranesStable charge separationParamagnetic resonance measurementsPhotosystem IIPSII samplesO2-evolving centerElectron transferCharge separationElectron donorNuclear hyperfine structureCytochrome b559Mn sitesResonance measurementsOxidationFraction of PSII
1985
Electron transfer in photosystem II at cryogenic temperatures.
De Paula J, Innes J, Brudvig G. Electron transfer in photosystem II at cryogenic temperatures. Biochemistry 1985, 24: 8114-20. PMID: 3004575, DOI: 10.1021/bi00348a042.Peer-Reviewed Original ResearchConceptsS2-state multiline EPR signalMultiline EPR signalElectron donationEPR signalS1 stateCytochrome b559Electron paramagnetic resonance spectroscopyParamagnetic resonance spectroscopyStable charge separationPhotosystem IIChemical oxidationChlorophyll cationElectron transferReaction center concentrationCharge separationElectron donorResonance spectroscopyS2 stateReaction centersTemperature rangeP680Signal speciesCenter concentrationB559Donation pathway