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Updated: Nov 23, 2025

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
Published on: September 23, 2021
Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts
Ornella Maglio1, Marco Chino2, Claudia Vicari2
1Department of Chemical Sciences, University Federico II of Naples, Via Cintia 21, Naples, 80126, Italy. alombard@unina.it and IBB-CNR, Via Mezzocannone 16, Naples, 80134, Italy.
Abstract:
Fe-Mimochrome VI*a is a synthetic peroxidase and peroxygenase, featuring two different peptides that are covalently-linked to deuteroheme. To perform a systematic structure/function correlation, we purposely shortened the distance between the distal peptide and the heme, allowing for the separation and characterization of two regioisomers. They differ in both His axial-ligand orientation, as determined by paramagnetic NMR shifts, and activity. These findings highlight that synthetic metalloenzymes may provide an efficient tool for disentangling the role of axial ligand orientation over peroxidase activity.
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