A Novel Tyrosine–Heme CO Covalent Linkage in F43Y Myoglobin: A New Post‐translational Modification of Heme Proteins

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...

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Bibliographic Details
Published in:ChemBioChem
Main Authors: Yan, Dao‐Jing, Li, Wei, Xiang, Yu, Wen, Ge‐Bo, Lin, Ying‐Wu, Tan, Xiangshi
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2014
Subjects:
Sperm whale
Online Access:http://dx.doi.org/10.1002/cbic.201402504
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcbic.201402504
https://onlinelibrary.wiley.com/doi/full/10.1002/cbic.201402504
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Summary: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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