Regulating the Heme Active Site by Covalent Modifications: Two Case Studies of Myoglobin

Chembiochem. 2023 Nov 28:e202300678. doi: 10.1002/cbic.202300678. Online ahead of print.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 F46C 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 activiation and peroxidase activity could be efficiently regulated, which suggests that this approach might be generally applied to the design of functional heme proteins.PMID:38015421 | DOI:10.1002/cbic.202300678

Source: Chembiochem - November 28, 2023 Category: Biochemistry Authors: Ze-Yuan Chen Hong Yuan Huamin Wang Li-Juan Sun Lu Yu Shu-Qin Gao Xiangshi Tan Ying-Wu Lin Source Type: research