A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins.
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.
School of Chemistry and Chemical Engineering, University of South China, Changsheng Road 28, Hengyang 421001 (China).
Dao-Jing
DJ
Yan
Wei
W
Li
Yu
Y
Xiang
Ge-Bo
GB
Wen
Ying-Wu
YW
Lin
Xiangshi
X
Tan
D019943:Amino Acid Substitution; D000818:Animals; D018360:Crystallography, X-Ray; D006418:Heme / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D010649:Phenylalanine / Q000737:chemistry*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D012996:Solutions; D013053:Spectrophotometry; D014443:Tyrosine / Q000737:chemistry*; D014907:Whales
D009211:Myoglobin; D012996:Solutions; D014443:Tyrosine; D006418:Heme; D010649:Phenylalanine; D006861:Hydrogen Peroxide
crosslinking; crystal structure; heme protein; post-translational modification; tyrosine-heme