A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold

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From: Journal of the American Chemical Society(Vol. 140, Issue 4)
Publisher: American Chemical Society
Document Type: Report
Length: 96 words

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Abstract :

The article demonstrates that installation of a noncanonical N'-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) reveals 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 afford efficient peroxidase biocatalysts within a globin fold, with activities comparable to those displayed by natureEs peroxidases.

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Gale Document Number: GALE|A534137650