Hidden route of protein damage through oxygen-confined photooxidation

Seoyoon Kim, Eojin Kim, Mingyu Park, Seong Ho Kim, Byung-Gyu Kim, Seungjin Na, Victor W. Sadongo, W. C. Bhashini Wijesinghe, Yu-Gon Eom, Gwangsu Yoon, Hannah Jeong, Eunhye Hwang, Chaiheon Lee, Kyungjae Myung, Chae Un Kim, Jeong-Mo Choi, Seung Kyu Min (), Tae-Hyuk Kwon () and Duyoung Min ()
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Seoyoon Kim: Ulsan National Institute of Science and Technology
Eojin Kim: Ulsan National Institute of Science and Technology
Mingyu Park: Ulsan National Institute of Science and Technology
Seong Ho Kim: Ulsan National Institute of Science and Technology
Byung-Gyu Kim: Institute for Basic Science
Seungjin Na: Korea Basic Science Institute
Victor W. Sadongo: Ulsan National Institute of Science and Technology
W. C. Bhashini Wijesinghe: Ulsan National Institute of Science and Technology
Yu-Gon Eom: Pusan National University
Gwangsu Yoon: Ulsan National Institute of Science and Technology
Hannah Jeong: Ulsan National Institute of Science and Technology
Eunhye Hwang: Ulsan National Institute of Science and Technology
Chaiheon Lee: Ulsan National Institute of Science and Technology
Kyungjae Myung: Institute for Basic Science
Chae Un Kim: Ulsan National Institute of Science and Technology
Jeong-Mo Choi: Pusan National University
Seung Kyu Min: Ulsan National Institute of Science and Technology
Tae-Hyuk Kwon: Ulsan National Institute of Science and Technology
Duyoung Min: Ulsan National Institute of Science and Technology

Nature Communications, 2024, vol. 15, issue 1, 1-19

Abstract: Abstract 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. Here, we report a hidden pathway of protein damage, which we refer to as O2-confined photooxidation. In this process, O2 is captured in protein cavities and subsequently converted into multiple ROS, primarily mediated by tryptophan residues under blue light irradiation. The generated ROS then attack the protein interior through constrained diffusion, causing protein damage. The effects of this photooxidative reaction appear to be extensive, impacting a wide range of cellular proteins, as supported by whole-cell proteomic analysis. This photooxidative mechanism may represent a latent oxidation pathway in human tissues directly exposed to visible light, such as skin and eyes.

Date: 2024
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DOI: 10.1038/s41467-024-55168-z

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