2002
Structure-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
Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II
Vrettos J, Reifler M, Kievit O, Lakshmi K, de Paula J, Brudvig G. Factors that determine the unusually low reduction potential of cytochrome c550 in cyanobacterial photosystem II. JBIC Journal Of Biological Inorganic Chemistry 2001, 6: 708-716. PMID: 11681704, DOI: 10.1007/s007750100249.Peer-Reviewed Original ResearchConceptsPCC 6803 photosystem IILow reduction potentialReduction potentialPyrolytic graphite edge electrodeElectron paramagnetic resonance spectroscopySquare wave voltammetryDirect electrochemical measurementsParamagnetic resonance spectroscopyBis-histidine axial ligationHeme reduction potentialCyanobacterial photosystem IIResonance Raman spectraPhotosystem IIWave voltammetryElectrode surfaceElectrochemistry experimentsElectrochemical measurementsElectrochemical valuesAxial ligationSolvent waterCyt c550Solvent exposureRedox titrationPeak separationPSII preparations
2000
Assignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †
Stewart D, Nixon P, Diner B, Brudvig G. Assignment of the Q y Absorbance Bands of Photosystem II Chromophores by Low-Temperature Optical Spectroscopy of Wild-Type and Mutant Reaction Centers †. Biochemistry 2000, 39: 14583-14594. PMID: 11087414, DOI: 10.1021/bi001246j.Peer-Reviewed Original ResearchMeSH KeywordsBacteriochlorophyllsBenzoquinonesCold TemperatureCyanobacteriaElectron Spin Resonance SpectroscopyFree RadicalsFreezingGlutamineHistidineLight-Harvesting Protein ComplexesMutagenesis, Site-DirectedOxidation-ReductionPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexSpectrophotometryTyrosineConceptsAbsorbance bandPhotosystem IIHydrogen bonding environmentOptical spectroscopyReaction center chromophoresRedox-active cofactorsDouble difference spectraLow temperature optical spectroscopyNumber of chromophoresRedox-active quinonesMutant reaction centersRedox stateRC chromophoresAxial ligandsCryogenic optical spectroscopyChromophore positionProtein environmentPSII preparationsSpectral assignmentsElectrochromic effectAccessory ChlElectronic structureChromophoreChromophore interactionsPhotosynthetic RCs
1998
Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †
Stewart D, Cua A, Chisholm D, Diner B, Bocian D, Brudvig G. Identification of Histidine 118 in the D1 Polypeptide of Photosystem II as the Axial Ligand to Chlorophyll Z †. Biochemistry 1998, 37: 10040-10046. PMID: 9665709, DOI: 10.1021/bi980668e.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonanceAxial ligandsChlorophyll ZPhotosystem IIRR spectraLow-temperature electron paramagnetic resonanceWild-type Photosystem IIRedox-active tyrosinesReaction centersEfficiency of photooxidationResonance Raman spectroscopyPSII complexesIR absorbance spectraD2 polypeptidesBacterial reaction centersParamagnetic resonanceRR signatureRaman spectroscopyAccessory ChlInfrared absorbanceQuantum yieldAbsorbance bandLigandsIR excitationLow-temperature illumination
1993
Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center.
Tang X, Chisholm D, Dismukes G, Brudvig G, Diner B. Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the photosystem II reaction center. Biochemistry 1993, 32: 13742-8. PMID: 8257709, DOI: 10.1021/bi00212a045.Peer-Reviewed Original Research