FEBS Letters · 1990 · 96 citations · 10 references
Natural SciencesBiochemistryBiophysicsMolecular BiophysicsSpectroscopyStructural BiologyBiophysical SpectroscopyConformational ChangeInfrared SpectroscopyOptical SpectroscopyProtein StructureSpectroscopy Of BiomoleculesConformational Transition StatesDifference SpectroscopyFourier TransformHydrogen Bonding InteractionsMacromolecular Structure CharacterizationProtein Backbone GeometryProtein Backbone Hydrogen BondsTransition States In Conformational Changes
A comparison is made between the PQA----P+QA- and PQAQB----P+QAQB-transitions in Rps. viridis and Rb. sphaeroides reaction centers (RCs) by the use of light-induced Fourier transform infrared (FTIR) difference spectroscopy. In Rb. sphaeroides RCs, we identify a signal at 1650 cm-1 which is present in the P+QA-minus-PQA spectrum and not in the P+QAQB(-)-minus-PQAQB spectrum. In contrast, this signal is present in both P+QA(-)-minus-PQA- and P+QAQB(-)-minus-PQAQB spectra of Rps. viridis RCs. These data are interpreted in terms of a conformational change of the protein backbone near QA (possible at the peptide C = O of a conserved alanine residue in the QA pocket) and of the different bonding interactions of QB with the protein in the RC of the two species.
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M. C. W. Evans · Nature · 1979 · 1.3K citations · Full text
James P. Allen, G. Fehér, Todd O. Yeates et al. · Proceedings of the National Academy of Sciences · 1988 · 298 citations · Full text
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