معرفی
Justin Bradley serves as a Research Fellow within the School of Chemistry, Pharmacy and Pharmacology at the University of East Anglia, actively contributing to biochemical research with emphasis on metalloprotein systems. His work is supported by current EPSRC funding for spectroscopic and synthetic facilities development through June 2026, following prior BBSRC-funded research on mitochondrial ferritin mechanisms (2017-2020).
His research focuses on iron metabolism and oxidative stress response in biological systems, particularly examining mitochondrial ferritin chemistry, iron-sulfur cluster dynamics, and metal-sensing transcriptional regulation. Key investigations include the unusual iron-O2 chemistry of human mitochondrial ferritin, assembly mechanisms of mineral cores in ferritin proteins, and redox properties of hemerythrin-like domains in plant proteins. This work bridges inorganic chemistry, structural biology, and cellular metabolism.
Recent publication trends (2025) demonstrate concentrated expertise in bioinorganic protein mechanisms, with articles appearing in high-impact journals including Nature Communications, Journal of the American Chemical Society, and Angewandte Chemie. His research consistently explores iron-based redox processes across bacterial, human, and plant systems, revealing fundamental principles of metal homeostasis and oxidative damage prevention.
Scientific contributions include:
- Mechanistic insights into mitochondrial ferritin's role in cellular iron metabolism
- Discovery of bacterioferritin-associated ferredoxin as a "biological fuse" against oxidative damage
- Characterization of iron-sensing properties in plant regulatory proteins
Bradley collaborates extensively within Professor Nick Le Brun's research group, contributing to projects examining iron-mediated oxidative stress responses and supramolecular systems. His technical expertise spans spectroscopic analysis, synthetic chemistry approaches, and structural characterization of metalloproteins, with current work focusing on nucleation site dynamics in ferritin proteins.
