Comparison of fluorescence properties of wild type and the W15F mutant of horse liver alcohol dehydrogenase

Maurice R. Eftink; Cing-Yuen Wong; Doo-Hong Park; Gretchen L. Shearer; Bryce V. Plapp

doi:10.1117/12.182716

17 August 1994 Comparison of fluorescence properties of wild type and the W15F mutant of horse liver alcohol dehydrogenase

Maurice R. Eftink, Cing-Yuen Wong, Doo-Hong Park, Gretchen L. Shearer, Bryce V. Plapp

Author Affiliations +

Proceedings Volume 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV; (1994) https://doi.org/10.1117/12.182716
Event: OE/LASE '94, 1994, Los Angeles, CA, United States

Abstract

Horse liver alcohol dehydrogenase is a homodimeric protein; each subunit has two tryptophan residues that are in distinctly different microenvironments. Trp-15 is located on the surface and Trp-314 is buried at the intersubunit interface. Steady-state and time-resolved fluorescence and phosphorescence studies have enabled the assignment of parameters, e.g., quantum yield, emission maximum, decay times, to the individual tryptophan residues of the protein. We have prepared, by site-directed mutagenesis, the mutated W15F protein and have characterized its fluorescence properties. We show that the Trp-314 of the mutant experiences an apolar microenvironment, but that the fluorescence decay and exposure to solute quenchers of the mutant are somewhat different than was expected from the assignments for the wild type.

Citation Download Citation

Maurice R. Eftink, Cing-Yuen Wong, Doo-Hong Park, Gretchen L. Shearer, and Bryce V. Plapp "Comparison of fluorescence properties of wild type and the W15F mutant of horse liver alcohol dehydrogenase", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); https://doi.org/10.1117/12.182716

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