PDBsum entry 5ojc

Oxidoreductase

PDB id: 5ojc

Contents

Protein chain

154 a.a.

Ligands

HEM-IMD

Waters ×143

PDB id:

5ojc

Name:

Oxidoreductase

Title:

Structure of mbq2.1 nmh

Structure:

Myoglobin. Chain: a. Engineered: yes

Source:

Physeter catodon. Sperm whale. Organism_taxid: 9755. Gene: mb. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.25Å R-factor: 0.194 R-free: 0.215

Authors:

T.Hayashi,M.Pott,T.Mori,P.Mittl,A.Green,D.Hivert

Key ref:

M.Pott et al. (2018). A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold. J Am Chem Soc, 140, 1535-1543. PubMed id: 29309143 DOI: 10.1021/jacs.7b12621

Date:

21-Jul-17 Release date: 24-Jan-18

Protein chain

P02185  (MYG_PHYMC) -  Myoglobin from Physeter macrocephalus

Seq: 154 a.a.

Struc: 154 a.a.*

* PDB and UniProt seqs differ at 11 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1021/jacs.7b12621

J Am Chem Soc 140:1535-1543 (2018)

PubMed id: 29309143

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

M.Pott, T.Hayashi, T.Mori, P.R.E.Mittl, A.P.Green, D.Hilvert.

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_δ-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.