PMID: 6411125Sep 14, 1983Paper

Segmental mobility in glycogen phosphorylase b

Biochimica Et Biophysica Acta
J MatkóB Somogyi

Abstract

The dynamics and structuredness of the pyridoxal 5'-phosphate-binding region in glycogen phosphorylase b (EC 2.4.1.1) has been investigated with different techniques of fluorescence spectroscopy. Fluorescence polarization data of the thermal Perrin plot indicate some mobility in the cofactor binding site, while the isothermic measurements (at 20 degrees C, in high-viscosity solvents) demonstrate that the mobile unit carrying the emission oscillator is practically insensitive to the external viscosity. Characteristics of the thermal Perrin plots obtained for both native and reduced phosphorylase b can be interpreted either as a freely moving cofactor in a medium of high viscosity (0.3 P) or as the motion of a unit larger than a lysine-bonded pyridoxal 5'-phosphate in a medium with the viscosity of water. Data for acrylamide quenching and time-resolved fluorescence measurements suggest that the latter interpretation should valid. These data also suggest a tightly packed microenvironment around the pyridoxal moiety.

References

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Citations

Jan 1, 1986·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·V DombrádiG Bot
Feb 16, 1999·Biochimica Et Biophysica Acta·S BenciP F Cook
Jul 31, 1984·Biochemical and Biophysical Research Communications·J MatkóB Somogyi
Nov 1, 1988·Quarterly Reviews of Biophysics·J MatkóS Damjanovich
Aug 30, 1996·Biophysical Chemistry·S VaccariA Mozzarelli

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