Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Publication Abstract from PubMed
The X-ray crystal structure of F43Y/T67R myoglobin revealed unique Tyr-heme double cross-links between Tyr43 and the heme 4-vinyl group, which represents a novel post-translational modification of heme proteins. Moreover, with the feature of a distal His-Arg pair, the designed artificial enzyme exhibited a peroxidase activity comparable to that of native peroxidases, such as the most efficient horseradish peroxidase.
Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases.,Liu C, Yuan H, Liao F, Wei CW, Du KJ, Gao SQ, Tan X, Lin YW Chem Commun (Camb). 2019 Jun 11;55(46):6610-6613. doi: 10.1039/c9cc02714a. Epub, 2019 May 23. PMID:31119219[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu C, Yuan H, Liao F, Wei CW, Du KJ, Gao SQ, Tan X, Lin YW. Unique Tyr-heme double cross-links in F43Y/T67R myoglobin: an artificial enzyme with a peroxidase activity comparable to that of native peroxidases. Chem Commun (Camb). 2019 Jun 11;55(46):6610-6613. doi: 10.1039/c9cc02714a. Epub, 2019 May 23. PMID:31119219 doi:http://dx.doi.org/10.1039/c9cc02714a
