A Novel Tyrosine–Heme CO 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 CO bond in an artificially produced sperm whale myoglobin (Mb) mutant, F43Y Mb, which formed spontaneously in vivo between the Tyr43...
Published in: | ChemBioChem |
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Main Authors: | , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2014
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Subjects: | |
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 |
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 CO 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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