Structural highlights
Function
[MYG_PHYCD] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Publication Abstract from PubMed
Expanding the range of genetically encoded metal coordination environments accessible within tunable protein scaffolds presents excellent opportunities for the creation of metalloenzymes with augmented properties and novel activities. Here, we demonstrate that installation of a noncanonical Ndelta-methyl histidine (NMH) as the proximal heme ligand in the oxygen binding protein myoglobin (Mb) leads to substantial increases in heme redox potential and promiscuous peroxidase activity. Structural characterization of this catalytically modified myoglobin variant (Mb NMH) revealed significant changes in the proximal pocket, including alterations to hydrogen-bonding interactions involving the prosthetic porphyrin cofactor. Further optimization of Mb NMH via a combination of rational modification and several rounds of laboratory evolution afforded efficient peroxidase biocatalysts within a globin fold, with activities comparable to those displayed by nature's peroxidases.
A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold.,Pott M, Hayashi T, Mori T, Mittl PRE, Green AP, Hilvert D J Am Chem Soc. 2018 Jan 19. doi: 10.1021/jacs.7b12621. PMID:29309143[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pott M, Hayashi T, Mori T, Mittl PRE, Green AP, Hilvert D. A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold. J Am Chem Soc. 2018 Jan 19. doi: 10.1021/jacs.7b12621. PMID:29309143 doi:http://dx.doi.org/10.1021/jacs.7b12621
