2023
Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium
Gisriel C, Elias E, Shen G, Soulier N, Flesher D, Gunner M, Brudvig G, Croce R, Bryant D. Helical allophycocyanin nanotubes absorb far-red light in a thermophilic cyanobacterium. Science Advances 2023, 9: eadg0251. PMID: 36961897, PMCID: PMC10038336, DOI: 10.1126/sciadv.adg0251.Peer-Reviewed Original ResearchConceptsFar-red lightLight-harvesting proteinsLight-harvesting phycobiliproteinsCryo-electron microscopyStructure-function relationshipsLow-light environmentsAP complexesThermophilic cyanobacteriumLow lightBiological plasticityPhotosystem I.Likely associatesAllophycocyaninParalogsEnhanced abilityCyanobacteriaCyanobacteriumAcclimationSubunitsPhycobiliproteinsProteinResource accessibilityDiversityAssemblesChlorophyll
2018
Engendering Methane Monooxygenase and Hydrogen Peroxide Oxidase Activity into a Designed Dimetal Protein by Increasing Protein Dynamics
Koder R, Preston J, Everson B, Bjerkefeldt E, Macazo F, Giroud F, Minteer S, Vinyard D, Brudvig G. Engendering Methane Monooxygenase and Hydrogen Peroxide Oxidase Activity into a Designed Dimetal Protein by Increasing Protein Dynamics. Biophysical Journal 2018, 114: 411a. DOI: 10.1016/j.bpj.2017.11.2276.Peer-Reviewed Original Research
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
1982
The nature of CuA in cytochrome c oxidase.
Stevens T, Martin C, Wang H, Brudvig G, Scholes C, Chan S. The nature of CuA in cytochrome c oxidase. Journal Of Biological Chemistry 1982, 257: 12106-12113. PMID: 6288707, DOI: 10.1016/s0021-9258(18)33685-8.Peer-Reviewed Original ResearchConceptsCytochrome c oxidaseYeast cytochrome c oxidaseC oxidaseCysteine sulfurProteinBeef heartOxidaseElectron nuclear double resonance (ENDOR) spectraElectron paramagnetic resonanceSubstantial spin densityParamagnetic resonanceDouble resonance spectraBetaCuAResonance spectraCysteineSpin densityHistidine