0000000000988643

AUTHOR

Sándor Száraz

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Structural factors controlling ligand binding to myoglobin: a kinetic hole-burning study.

1998

Using temperature-derivative spectroscopy in the temperature range below 100 K, we have studied the dependence of the Soret band on the recombination barrier in sperm whale carbonmonoxy myoglobin (MbCO) after photodissociation at 12 K. The spectra were separated into contributions from the photodissociated species, Mb*CO, and CO-bound myoglobin. The line shapes of the Soret bands of both photolyzed and liganded myoglobin were analyzed with a model that takes into account the homogeneous bandwidth, coupling of the electronic transition to vibrational modes, and static conformational heterogeneity. The analysis yields correlations between the activation enthalpy for rebinding and the model p…

MaleMultidisciplinaryBinding SitesProtein ConformationSpectrum AnalysisPhotodissociationEnthalpyWhalesBiological SciencesLigandsSpermatozoaMolecular electronic transitionSpectral lineCrystallographychemistry.chemical_compoundMyoglobinchemistryChemical physicsMolecular vibrationAnimalsSpectroscopyMetmyoglobinHemeProtein BindingProceedings of the National Academy of Sciences of the United States of America
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