2021
The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase
Li Y, Valdez NA, Mnatsakanyan N, Weber J. The nucleotide binding affinities of two critical conformations of Escherichia coli ATP synthase. Archives Of Biochemistry And Biophysics 2021, 707: 108899. PMID: 33991499, PMCID: PMC8278868, DOI: 10.1016/j.abb.2021.108899.Peer-Reviewed Original ResearchMeSH KeywordsCatalytic DomainEscherichia coliModels, MolecularNucleotidesProtein BindingProton-Translocating ATPasesConceptsATP synthaseCritical conformationEscherichia coli ATP synthaseRotary catalytic mechanismCatalytic dwell stateCatalytic mechanismAerobic energy metabolismΓ subunitCysteine mutationsTryptophan fluorescenceDwell stateDisulfide bondsEnergetic functionEnergy metabolismCatalytic siteSynthaseCatalytic dwellAffinity changesATPEnzymeAffinityConformationSubunitsMutationsSites
2011
The β Subunit Loop That Couples Catalysis and Rotation in ATP Synthase Has a Critical Length*
Mnatsakanyan N, Kemboi SK, Salas J, Weber J. The β Subunit Loop That Couples Catalysis and Rotation in ATP Synthase Has a Critical Length*. Journal Of Biological Chemistry 2011, 286: 29788-29796. PMID: 21705326, PMCID: PMC3191020, DOI: 10.1074/jbc.m111.254730.Peer-Reviewed Original Research