A comparison study on ribonuclease A modifications induced by substituted p-benzoquinones

Bioorganic Chemistry
Jisook KimDawn M Stickle

Abstract

In this paper, we present our investigation on ribonuclease A (RNase) modifications induced by 1,4-benzoquinone (PBQ), 2-methyl-1,4-benzoquinone (MBQ), and 2-chloro-1,4-benzoquinone (CBQ). The goal of the study was to evaluate quinone-induced protein modifications as well as substituent effects, utilizing several techniques such as SDS-PAGE, fluorescence spectroscopy, microscopy, and LC-ESI(+)-QTOF-MS. SDS-PAGE experiments revealed that all quinones modify RNase through oligomerization as well as polymeric aggregation; with CBQ functioning as the most efficient quinone while MBQ was least efficient. The fluorescence emission was found to be less intense and the anisotropy values were found to be slightly higher for the modified RNase compared to the unmodified RNase. UV-Vis spectroscopy indicated that all three quinones formed adducts in which they were covalently linked to RNase. Confocal imaging analysis showed that the presence of CBQ resulted in massive RNase aggregation, while PBQ-treated RNase formed much smaller aggregates. MBQ-treated RNase exhibited micrographic features that closely resembled those of the unmodified RNase. LC-ESI(+)-QTOF-MS studies indicated the nature of PBQ- and CBQ-induced RNase modifications are c...Continue Reading

References

Dec 1, 1996·Environmental Health Perspectives·R Snyder, C C Hedli
Dec 11, 1999·Nucleic Acids Research·A Bairoch, R Apweiler
Apr 30, 2002·Free Radical Biology & Medicine·Shosuke KawanishiShinji Oikawa
Jan 25, 2008·BMC Bioinformatics·Yang Zhang

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