期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 140, 期 4, 页码 1535-1543出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b12621
关键词
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资金
- ETH Zurich
- Swiss National Science Foundation
- JSPS fellowship
- Biotechnology and Biological Sciences Research Council [BB/M027023/1]
- UK Catalysis Hub - EPSRC [EP/K014706/2, EP/K014668/1, EP/K014854/1, EP/K014714/1, EP/M013219/1]
- BBSRC [BB/M017702/1, BB/M027023/1] Funding Source: UKRI
- EPSRC [EP/M013219/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/M017702/1] Funding Source: researchfish
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 N-delta-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.
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