6533b821fe1ef96bd127b8f8

RESEARCH PRODUCT

Unveiling the timescale of the R-T transition in human hemoglobin.

Michael WulffMatteo LevantinoMarco CammarataAntonio Cupane

subject

PhotochemistryProtein ConformationKineticsMethemoglobinHemoglobinsStructural BiologyHumansScattering RadiationSpectroscopyMolecular BiologyallosteryScatteringChemistryProtein dynamicsSpectrum AnalysisPhotodissociationhemoglobinHydrogen-Ion ConcentrationSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CrystallographyKineticsStructural changeChemical physicshemoglobin; allostery; protein dynamicsprotein dynamicssense organsHemoglobin

description

Time-resolved wide-angle X-ray scattering, a recently developed technique allowing to probe global structural changes of proteins in solution, was used to investigate the kinetics of R-T quaternary transition in human hemoglobin and to systematically compare it to that obtained with time-resolved optical spectroscopy under nearly identical experimental conditions. Our data reveal that the main structural rearrangement associated with the R-T transition takes place approximately 2 mus after the photolysis of hemoglobin at room temperature and neutral pH. This finding suggests that the 20-mus step observed with time-resolved optical spectroscopy corresponds to a small and localized structural change.

yearjournalcountryeditionlanguage
2010-01-27Journal of molecular biology
10.1016/j.jmb.2010.05.057https://pubmed.ncbi.nlm.nih.gov/20553731