Affiliation:
1. School of Chemistry and Chemical Engineering University of South China Hengyang 421001 China
2. Department of Chemistry & Institute of Biomedical Science Fudan University Shanghai 200433 China
3. Hengyang Medical School University of South China Hengyang 421001 China
4. High Magnetic Field Laboratory Chinese Academy of Sciences Hefei Anhui 230031 China
Abstract
AbstractUsing myoglobin (Mb) as a model protein, we herein developed a facial approach to modifying the heme active site. A cavity was first generated in the heme distal site by F46 C mutation, and the thiol group of Cys46 was then used for covalently linked to exogenous ligands, 1H‐1,2,4‐triazole‐3‐thiol and 1‐(4‐hydroxyphenyl)‐1H‐pyrrole‐2,5‐dione. The engineered proteins, termed F46C‐triazole Mb and F46C‐phenol Mb, respectively, were characterized by X‐ray crystallography, spectroscopic and stopped‐flow kinetic studies. The results showed that both the heme coordination state and the protein function such as H2O2 activation and peroxidase activity could be efficiently regulated, which suggests that this approach might be generally applied to the design of functional heme proteins.
Funder
National Natural Science Foundation of China
Subject
Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry