%0 Journal Article
%T A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins.
%A Yan DJ
%A Li W
%A Xiang Y
%A Wen GB
%A Lin YW
%A Tan X
%J Chembiochem
%V 16
%N 1
%D Jan 2015 2
%M 25392956
%F 3.461
%R 10.1002/cbic.201402504
%X Heme post-translational modification plays a key role in tuning the structure and function of heme proteins. We herein report a novel tyrosine-heme covalent C−O bond in an artificially produced sperm whale myoglobin (Mb) mutant, F43Y Mb, which formed spontaneously in vivo between the Tyr43 hydroxy group and the heme 4-vinyl group. This highlights the diverse chemistry of heme post-translational modifications, and lays groundwork for further investigation of the structural and functional diversity of covalently-bound heme proteins.