1996
Reversible Binding of Nitric Oxide to Tyrosyl Radicals in Photosystem II. Nitric Oxide Quenches Formation of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II†
Szalai V, Brudvig G. Reversible Binding of Nitric Oxide to Tyrosyl Radicals in Photosystem II. Nitric Oxide Quenches Formation of the S3 EPR Signal Species in Acetate-Inhibited Photosystem II†. Biochemistry 1996, 35: 15080-15087. PMID: 8942675, DOI: 10.1021/bi961117w.Peer-Reviewed Original ResearchConceptsS3 EPR signalOxygen-evolving complexMultiline EPR signalEPR signalS2 statePhotosystem IIManganese-depleted photosystem IIS2-state multiline EPR signalRedox-active tyrosinesPhotosystem II samplesRadical EPR signalSignal speciesNitric oxide (NO) bindsTyrosyl radicalsAmmonia resultsReversible bindingOxideYZDipolar interactionsRibonucleotide reductase
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