A Novel Tyrosine–Heme CO Covalent Linkage in F43Y Myoglobin: A New Post‐translational Modification of Heme Proteins |
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| Authors: | Dao‐Jing Yan Dr Wei Li Dr Yu Xiang Prof Dr Ge‐Bo Wen Prof Dr Ying‐Wu Lin Prof Dr Xiangshi Tan |
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| Affiliation: | 1. School of Chemistry and Chemical Engineering, University of South China, Changsheng Road 28, Hengyang 421001 (China);2. Department of Chemistry, Institute of Biomedical Science, Fudan University, Handan Road 220, Shanghai 200433 (China);3. Department of Chemistry, Tsinghua University, Shuangqing Road 30, Beijing 100083 (China);4. Laboratory of Protein Structure and Function, University of South China, Changsheng Road 28, Hengyang 421001 (China) |
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| Abstract: | 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. |
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| Keywords: | crosslinking crystal structure heme protein post‐translational modification tyrosine– heme |
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