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  • Title: Phosphorescence properties of Trp-84 and Trp-310 in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus.
    Author: Gabellieri E, Strambini GB.
    Journal: Biophys Chem; 1989 Jul; 33(3):257-64. PubMed ID: 2804244.
    Abstract:
    The phosphorescence spectra of Trp-84 and Trp-310 in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus in an aqueous glass show distinct 0,0 vibrational bands with peaks at 406.5 and 410.5 nm. With the aid of external heavy-atom perturbation of iodide and the thermal quenching profile, it is concluded that although both chromophores are effectively buried, only one, viz., the 406.5 nm component, is embedded in a sufficiently rigid core of the protein to phosphoresce in fluid solutions at room temperature. From inspection of the crystallographic structure is it evident that only Trp-310 embedded in the beta-sheet of the catalytic domain may satisfy the requirements of a long triplet-state lifetime and slow migration of O2 to its site. This identification confirms previous analysis of the phosphorescence properties of the enzymes from yeast, pig and rabbit muscle.
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