Hidden route of protein damage through oxygen-confined photooxidation

Authors: Kim S, Kim E, Park M, Kim SH, Kim BG, Na S, Sadongo VW, Wijesinghe WCB, Eom YG, Yoon G, Jeong H, Hwang E, Lee C, Myung K, Kim CU, Choi JM, Min SK, Kwon TH, Min D

Year: 2024 Dec 30

Category: Biochemistry

Journal: Nature Communications

DOI: 10.1038/s41467-024-55168-z

URL: https://www.nature.com/articles/s41467-024-55168-z

Abstract

Overview

Oxidative modifications can disrupt protein folds and functions, and are strongly associated with human aging and diseases.

Conventional oxidation pathways typically involve the free diffusion of reactive oxygen species (ROS), which primarily attack the protein surface. Yet, it remains unclear whether and how internal protein folds capable of trapping oxygen (O2) contribute to oxidative damage.

Findings

  • Hidden Pathway Identified: The study reports a hidden pathway of protein damage called O2-confined photooxidation.
  • Mechanism: In this process, oxygen (O2) is captured in protein cavities and converted into multiple ROS, mediated by tryptophan residues under blue light irradiation.
  • Impact: The generated ROS attack the protein interior through constrained diffusion, causing extensive protein damage.
  • Proteomic Evidence: Whole-cell proteomic analysis supports that this photooxidative reaction affects a wide range of cellular proteins.

Conclusion

This photooxidative mechanism represents a latent oxidation pathway, which is especially relevant in human tissues directly exposed to visible light, such as skin and eyes. The connection between electromagnetic field (EMF) exposure (specifically blue light) and protein/oxidative damage is emphasized, highlighting potential health risks and cellular impacts in exposed tissues.

protein damage photooxidation reactive oxygen species blue light oxidative stress cellular proteins visible light exposure
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