Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts

Ornella Maglio, Marco Chino, Claudia Vicari, Vincenzo Pavone, Ricardo O. Louro, Angela Lombardi

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)990-993
Number of pages4
JournalChemical Communications
Volume57
Issue number8
DOIs
Publication statusPublished - 25 Jan 2021

Fingerprint

Dive into the research topics of 'Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts'. Together they form a unique fingerprint.

Cite this