Publication: A noncanonical proximal heme ligand affords an efficient peroxidase in a globin fold
A noncanonical proximal heme ligand affords an efficient peroxidase in a globin fold
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Pott, M., Hayashi, T., Mori, T., Mittl, P. R. E., Green, A. P., & Hilvert, D. (2018). A noncanonical proximal heme ligand affords an efficient peroxidase in a globin fold. Journal of the American Chemical Society, 140, 1535–1543. https://doi.org/10.1021/jacs.7b12621
Abstract
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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 Nδ-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 modifie
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Creators (Authors)
- Pott, Moritz
- Hayashi, Takahiro
- Mori, Takahiro
- Mittl, Peer R E
- Green, Anthony P
- Hilvert, Donald
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Citations
Pott, M., Hayashi, T., Mori, T., Mittl, P. R. E., Green, A. P., & Hilvert, D. (2018). A noncanonical proximal heme ligand affords an efficient peroxidase in a globin fold. Journal of the American Chemical Society, 140, 1535–1543. https://doi.org/10.1021/jacs.7b12621
