The broad diversity of heme-protein cross-links: An overview.
Heme proteins perform a large array of biological functions using the same heme cofactor. A primary method of regulating these diverse functions is the heme-protein cross-link, an important post-translational modification. This review presents an overview of the broad diversity of heme-protein cross-links, including Cys/SeCys -heme, Met-heme, His-heme, Trp/Tyr-heme, Glu/Asp-heme and Lys-heme cross-links, which have been discovered in the last three decades, with bond type ranging from C-S, C-Se, C-N, C-C to C-O. Many advances have been made in revealing the mechanisms of heme-protein cross-link formation, as well as the structural and functional roles. Moreover, most of these cross-links have been successfully recreated in natural or de novo proteins. These tremendous progresses have not only enhanced our knowledge of how cross-links fine-tune the structure and function of natural heme proteins, but also provided us powerful strategies for design of artificial heme proteins with functionalities beyond those of natural heme proteins.
School of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China; Laboratory of Protein Structure and Function, University of South China, Hengyang 421001, China. Electronic address: linlinying@hotmail.com.
Ying-Wu
YW
Lin
D000818:Animals; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism
D011506:Proteins; D006418:Heme
Compound I; Cross-link; Heme protein; Post-translational modifications; Protein design