Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Publication Abstract from PubMed
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.
A Novel Tyrosine-Heme CO Covalent Linkage in F43Y Myoglobin: A New Post-translational Modification of Heme Proteins.,Yan DJ, Li W, Xiang Y, Wen GB, Lin YW, Tan X Chembiochem. 2015 Jan 2;16(1):47-50. doi: 10.1002/cbic.201402504. Epub 2014 Nov, 12. PMID:25392956[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yan DJ, Li W, Xiang Y, Wen GB, Lin YW, Tan X. A Novel Tyrosine-Heme CO Covalent Linkage in F43Y Myoglobin: A New Post-translational Modification of Heme Proteins. Chembiochem. 2015 Jan 2;16(1):47-50. doi: 10.1002/cbic.201402504. Epub 2014 Nov, 12. PMID:25392956 doi:http://dx.doi.org/10.1002/cbic.201402504