Abstract 2766 Exploring the Functional Diversity of Ferredoxin-Thioredoxin Reductase Domain-Containing Proteins
Thioredoxin systems are vital for reducing target proteins, crucial in maintaining cellular homeostasis and redox signaling across various life forms. These systems consist of thioredoxin (Trx) and the corresponding thioredoxin reductase (TrxR), which reduces Trx. Trx contains a conserved Cys-XX-Cys motif that forms a redox-active disulfide, enabling the reduction of disulfides in target proteins through a dithiol-disulfide exchange mechanism. Although these systems are uniformly distributed across all life forms, significantly less is known about the biochemistry and physiology of Trx/TrxR enzymes in organisms from the Archaea and Bacteria domains.
Authors
- Amit Rai (ORCID: https://orcid.org/0000-0002-5715-8541)
- Yisong Guo (ORCID: https://orcid.org/0000-0002-4132-3565)
- Jin Xiong (ORCID: https://orcid.org/0000-0001-7443-0554)
- Neelima Bhatt
- Divya Prakash (ORCID: https://orcid.org/0000-0003-0080-2583)
- Sukhpal Bhullar
Institutions
- Southern Illinois University Carbondale (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.110028
- Primary Topic
- Redox biology and oxidative stress
- Type
- article
- Field-Weighted Citation Impact
- 0.00