Photo-oxidation of lysozyme triggered by riboflavin is O2-dependent, occurs via mixed type 1 and type 2 pathways, and results in inactivation, site-specific damage and intra- and inter-molecular crosslinks.

Free Radical Biology & Medicine
Eduardo Fuentes-LemusCamilo Lopez-Alarcon

Abstract

Photosensitized protein oxidation is a promising tool for medical procedures such as photochemical tissue bonding (PTB). We have recently reported that the binding of rose Bengal, a sensitizer employed in PTB, to lysozyme modulates the photooxidation and crosslinking of this protein. In this work we examined the photooxidation and crosslinking of lysozyme mediated by riboflavin (RF) an endogenous sensitizer also employed in PTB. We hypothesized that since RF does not bind strongly to proteins, the mechanism(s) and extent of enzymatic inactivation, amino acid modification and protein crosslinking would be dependent on the presence of O2, and differ to that induced by rose Bengal. This hypothesis was tested using UV-visible spectrophotometry, isothermal titration calorimetry (ITC), SDS-PAGE gels, quantification of amino acid consumption, and LC-MS analysis of sites of modification and crosslinks. Under N2, limited damage was detected arising from type 1 (radical) chemistry with formation of specific intra- (Tyr20-Tyr23) and inter- (Tyr23-Trp108) molecular crosslinks. In contrast, the presence of O2 triggered extensive protein damage through mixed type 1 and type 2 (1O2) mechanisms leading to Trp, Met, Tyr and His oxidation, loss ...Continue Reading

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Citations

Sep 29, 2020·Frontiers in Cell and Developmental Biology·Tirthankar SinhaMuayyad R Al-Ubaidi
Feb 5, 2021·Physical Chemistry Chemical Physics : PCCP·Jianfeng ZhaoDavid Lee Phillips
Nov 21, 2020·Free Radical Biology & Medicine·Anouchka GatinCécile Sicard-Roselli
Feb 19, 2021·Redox Biology·Shuwen JiangMichael J Davies
Jun 17, 2021·Photochemistry and Photobiology·Maurício S BaptistaAndrés H Thomas

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