2023
A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center
Gisriel C, Flesher D, Long Z, Liu J, Wang J, Bryant D, Batista V, Brudvig G. A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center. Photosynthesis Research 2023, 1-10. PMID: 37749456, DOI: 10.1007/s11120-023-01047-5.Peer-Reviewed Original ResearchCryo-EM mapsCryogenic electron microscopy structureReaction centersHydrogen bond donorCryo-EM structureElectron microscopy structureReaction center complexBond donorPhotosynthetic organismsMicroscopy structureProtein complexesElectron transferMolecular structureFunctional insightsStructural biologyLight harvestingProtein environmentChemical environmentExperimental cryo-EM mapsDownstream investigationsCenter complexPrimary pigmentEnergy transferStructural dataAcetyl moiety
2022
Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light
Gisriel C, Shen G, Flesher D, Kurashov V, Golbeck J, Brudvig G, Amin M, Bryant D. Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light. Journal Of Biological Chemistry 2022, 299: 102815. PMID: 36549647, PMCID: PMC9843442, DOI: 10.1016/j.jbc.2022.102815.Peer-Reviewed Original ResearchConceptsFar-red light photoacclimationChl dFar-red lightPhotosystem IIChl fWater-splitting enzymeEnergy transferDimeric photosystem II complexesCryo-EM structurePhotosystem II complexElectron transfer chainWater oxidationChl f moleculesDimeric complexStructure-function relationshipsPhotosynthetic machineryPsbH subunitProtein environmentMonomeric structureOxygenic photosynthesisVisible lightFormyl moietyF moleculesAccessory pigmentsTransfer chain
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
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