Polycyclic aromatic hydrocarbons are a group of chemicals, that can be toxic to the environment. These environmental pollutants can be released in a variety of ways, and their toxicity is thought to emerge from some of their metabolites, particularly quinones. In this study we present our research on modifications of ribonuclease A or lysozyme induced by 1,4-benzoquinone, 1,2-naphthoquinone, 1,4-naphthoquinone, and 2-hydroxy-1,4-naphthoquinone. These protein modifications were monitored by utilizing fluorescence and UV-Vis spectroscopy techniques. The modifications were characterized by a reduced fluorescence of the protein compared to the unmodified protein and an increased absorbance in UV-Vis due to an adduct formation of the quinone with the protein. Various reaction conditions were investigated including different concentrations of the quinone and protein, the pH of the solution, the temperature, and the presence of metal ions. This study further expands our knowledge of the severity of quinones impact on the environment as well as cellular proteins.

Fluorescence and UV-Vis studies of quinone-induced protein modifications

256th National Meeting (2018)

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