5OJC

Structure of MbQ2.1 NMH

5OJC の概要

• エントリーDOI: 10.2210/pdb5ojc/pdb
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, IMIDAZOLE, ... (4 entities in total)
• 機能のキーワード: myoglobin, nmh, n-methylhistidine, heme, oxidoreductase
• 由来する生物種: Physeter catodon (Sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18925.49

構造登録者

Hayashi, T.,Pott, M.,Mori, T.,Mittl, P.,Green, A.,Hivert, D. (登録日: 2017-07-21, 公開日: 2018-01-24, 最終更新日: 2024-01-17)

主引用文献

Pott, M.,Hayashi, T.,Mori, T.,Mittl, P.R.E.,Green, A.P.,Hilvert, D.
A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold.
J. Am. Chem. Soc., 140:1535-1543, 2018

PubMed Abstract: 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-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.

PubMed: 29309143
DOI: 10.1021/jacs.7b12621

実験手法

X-RAY DIFFRACTION (1.25 Å)