Evidence for reversible excited-state process in tryptophan zwitterion

Noel Boens; Luc Van Dommelen; Frans C. De Schryver; Marcel Ameloot

doi:10.1117/12.182749

17 August 1994 Evidence for reversible excited-state process in tryptophan zwitterion

Noel Boens, Luc Van Dommelen, Frans C. De Schryver, Marcel Ameloot

Proceedings Volume 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV; (1994) https://doi.org/10.1117/12.182749
Event: OE/LASE '94, 1994, Los Angeles, CA, United States

Abstract

This report gives evidence that the biexponential fluorescence decay of tryptophan zwitterion in H₂O solution is due to the occurrence of a reversible two-state excited-state process whereby the corresponding ground-state species are excited. The rate constants are within the intervals: 0<k₀₁<0.57(ns)^-1, 0.76(ns)^-1<k₂₁<1.33(ns)^-1, 0<k₀₂<0.58(ns)^-1, 0.77(ns)^-1<k₁₂<1.35(ns)^-1. These limits were calculated using the values for S₁ equals k₀₁ + k₂₁ (1.33+/- 0.01(ns)^-1), S₂ equals k₀₂ + k₁₂(1.35+/- 0.01(ns)^-1), and P equals k₂₁k₁₂(1.03+/- 0.01(ns)^-2). The emission spectra of the two excited-state species can be uniquely determined and are different from those associated with the decay times. These results were obtained by repetitive global compartmental analyses of the fluorescence decay surface of tryptophan zwitterion measured over the entire emission spectrum as a function of quencher concentration. This new and powerful analysis method is applicable to all biexponential protein fluorescence decays.

Citation Download Citation

Noel Boens, Luc Van Dommelen, Frans C. De Schryver, and Marcel Ameloot "Evidence for reversible excited-state process in tryptophan zwitterion", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); https://doi.org/10.1117/12.182749

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