2024
Mutation-induced shift of the photosystem II active site reveals insight into conserved water channels
Flesher D, Liu J, Wang J, Gisriel C, Yang K, Batista V, Debus R, Brudvig G. Mutation-induced shift of the photosystem II active site reveals insight into conserved water channels. Journal Of Biological Chemistry 2024, 300: 107475. PMID: 38879008, PMCID: PMC11294709, DOI: 10.1016/j.jbc.2024.107475.Peer-Reviewed Original ResearchOxygen-evolving complexPhotosystem II active sitePhotosystem IIJahn-Teller distortionPhotosystem II complexD1-Asp170Jahn-TellerResolution cryo-EM structureMutation-induced structural changesCryo-EM structureMagnetic propertiesD1 subunitActive siteOxygenic photosynthesisMutagenesis studiesLight-driven water oxidationSpectroscopic propertiesStructural basisSpectroscopic dataAmino acidsWater oxidation mechanismPhotosystemMutationsMutation-induced shiftWater oxidation
2021
Enhanced specificity mutations perturb allosteric signaling in CRISPR-Cas9
Nierzwicki L, East K, Morzan U, Arantes P, Batista V, Lisi G, Palermo G. Enhanced specificity mutations perturb allosteric signaling in CRISPR-Cas9. ELife 2021, 10: e73601. PMID: 34908530, PMCID: PMC8741213, DOI: 10.7554/elife.73601.Peer-Reviewed Original ResearchConceptsHNH domainAllosteric communicationCatalytic HNH domainDNA recognition regionSpecificity-enhancing mutationsGenome editing capabilitiesAllosteric signalingAllosteric signalMutations perturbAllosteric hotspotsSpecificity enhancementCas9 endonucleaseMutational studiesDNA recognitionAllosteric connectivityAllosteric roleMolecular toolsAllosteric structureRecognition regionMolecular levelBiochemical studiesDNA cleavageSolution NMRMutationsCatalytic site
2013
Spectral Tuning of Ultraviolet Cone Pigments: An Interhelical Lock Mechanism
Sekharan S, Mooney V, Rivalta I, Kazmi M, Neitz M, Neitz J, Sakmar T, Yan E, Batista V. Spectral Tuning of Ultraviolet Cone Pigments: An Interhelical Lock Mechanism. Journal Of The American Chemical Society 2013, 135: 19064-19067. PMID: 24295328, PMCID: PMC4536979, DOI: 10.1021/ja409896y.Peer-Reviewed Original ResearchConceptsUV pigmentsCone pigmentsSpectral tuningActivation of rhodopsinAncestral pigmentMolecular evolutionVertebrate visionMutagenesis studiesPhotoreceptor rhodopsinMolecular levelStructural rearrangementsUnprotonated Schiff baseTransmembraneTM6PigmentsRhodopsinMutationsEssential componentRetinyl chromophoreHydrogen bonding networkMutantsTM2Structural modelPhysiologicalRearrangementSpectral Tuning in Halorhodopsin: The Chloride Pump Photoreceptor
Pal R, Sekharan S, Batista V. Spectral Tuning in Halorhodopsin: The Chloride Pump Photoreceptor. Journal Of The American Chemical Society 2013, 135: 9624-9627. PMID: 23777372, DOI: 10.1021/ja404600z.Peer-Reviewed Original ResearchConceptsKey amino acid residuesIon translocation pathwayAmino acid residuesSpectral tuningInternal water moleculesTranslocation pathwaySpecific hydrogen bondsHalobacterium salinarumAcid residuesMolecular levelStructural rearrangementsAnion transportCl depletionPhotoreceptorsInduces changesHalorhodopsinRetinyl chromophoreSalinarumMutationsResiduesPathwayFirst time
2012
The Active Site of Melanopsin: The Biological Clock Photoreceptor
Sekharan S, Wei J, Batista V. The Active Site of Melanopsin: The Biological Clock Photoreceptor. Journal Of The American Chemical Society 2012, 134: 19536-19539. PMID: 23145979, DOI: 10.1021/ja308763b.Peer-Reviewed Original Research