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PDBsum entry 5ojc
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Oxidoreductase
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PDB id
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5ojc
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References listed in PDB file
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Key reference
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Title
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A noncanonical proximal heme ligand affords an efficient peroxidase in a globin fold.
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Authors
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M.Pott,
T.Hayashi,
T.Mori,
P.R.E.Mittl,
A.P.Green,
D.Hilvert.
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Ref.
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J Am Chem Soc, 2018,
140,
1535-1543.
[DOI no: ]
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PubMed id
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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 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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