2011
Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II
Pokhrel R, McConnell IL, Brudvig GW. Chloride Regulation of Enzyme Turnover: Application to the Role of Chloride in Photosystem II. Biochemistry 2011, 50: 2725-2734. PMID: 21366335, DOI: 10.1021/bi2000388.Peer-Reviewed Original ResearchConceptsOxygen-evolving complexPhotosystem IICatalytic residuesChloride-binding siteRecent structural evidenceCyanobacterial photosystem IISalt bridgeEnzyme-substrate complexΑ-amylaseResidue crucialConformational shiftS-state cycleLys residuesCarboxylate residuesEnzyme turnoverChloride regulationResiduesD61Structural evidenceManganese clusterEnzymeBindingD1Potential mechanismsArg
2004
Structure-based mechanism of photosynthetic water oxidation
McEvoy J, Brudvig G. Structure-based mechanism of photosynthetic water oxidation. Physical Chemistry Chemical Physics 2004, 6: 4754-4763. DOI: 10.1039/b407500e.Peer-Reviewed Original ResearchOxygen-evolving complexO bond-forming stepSubstrate water moleculesX-ray crystal structureBond-forming stepPhotosynthetic water oxidationWater splitting reactionResolution X-ray crystal structureCyanobacterial photosystem IIÅ resolution X-ray crystal structureCP43-Arg357Water oxidationStructure-based mechanismWater moleculesCertain amino acid residuesAmino acid residuesCrystal structureMechanistic functionPhotosystem IIArginine residuesCrystallographic informationLends weightResiduesNucleophilesOxidation
1999
Mapping RNA−Protein Interactions in Ribonuclease P from Escherichia coli Using Electron Paramagnetic Resonance Spectroscopy †
Gopalan V, Kühne H, Biswas R, Li H, Brudvig G, Altman S. Mapping RNA−Protein Interactions in Ribonuclease P from Escherichia coli Using Electron Paramagnetic Resonance Spectroscopy †. Biochemistry 1999, 38: 1705-1714. PMID: 10026248, DOI: 10.1021/bi9807106.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBinding SitesComputer SimulationElectron Spin Resonance SpectroscopyEndoribonucleasesEscherichia coliEscherichia coli ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein FoldingRibonuclease PRibonucleoproteinsRNA, BacterialRNA, CatalyticSpin LabelsStructure-Activity RelationshipConceptsM1 RNAC5 proteinRibonuclease PCysteine residuesEscherichia coliRNA-protein interfaceCatalytic RNA subunitNative cysteine residuesSulfhydryl-specific reagentsCatalytic ribonucleoproteinRNA subunitHoloenzyme complexRNP complexesProtein cofactorsMutant derivativesDeletion derivativesRNASpin labelsProteinSpectroscopy-based approachRibonucleoproteinResiduesPosition 16Coli