Two-dimensional fluorescence correlation spectroscopy IV: resolution of fluorescence of tryptophan residues in alcohol dehydrogenase and lysozyme

Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy
Hiroaki FukumaIsao Noda

Abstract

Generalized two-dimensional (2D) fluorescence correlation spectroscopy has been used to resolve the fluorescence spectra of two tryptophan (Trp) residues in alcohol dehydrogenase and lysozyme. In each protein, one Trp residue is buried in a hydrophobic domain of the protein matrix and the other Trp residue is located at a hydrophilic domain close to the protein-water interface. Fluorescence quenching by iodide ion, a hydrophilic quencher, was employed as a perturbation to induce the intensity change in the spectra. The Trp residue which is located at the hydrophilic domain is effectively quenched by the quencher, while the Trp residue located at the hydrophobic domain is protected from the quenching. Therefore, the fluorescence of these two Trp residues have a different sensitivity to the quenching, showing a different response to the concentration of the quencher. Fluorescence spectra of the two Trp residues in alcohol dehydrogenase, which are heavily overlapped in conventional one-dimensional spectra, have been successfully resolved by the 2D correlation technique. From the asynchronous correlation map, it was revealed that the quenching of Trp located at the hydrophobic part was brought about after that of Trp located at the...Continue Reading

Citations

Sep 22, 2015·Langmuir : the ACS Journal of Surfaces and Colloids·Peng-Fan GaoLixin Wu
Oct 20, 2018·Angewandte Chemie·Luca BuzzettiPaolo Melchiorre
Mar 3, 2020·Analytical Sciences : the International Journal of the Japan Society for Analytical Chemistry·Mengmeng HeShin-Ichi Morita
Nov 20, 2016·Wiley Interdisciplinary Reviews. Nanomedicine and Nanobiotechnology·Ran Chen, Jim E Riviere
Jul 8, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Edward KrzyżakAleksandra Marciniak

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