Issue 8, 2021

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

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.

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

Supplementary files

Article information

Article type
Communication
Submitted
06 oct. 2020
Accepted
22 déc. 2020
First published
22 déc. 2020

Chem. Commun., 2021,57, 990-993

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

O. Maglio, M. Chino, C. Vicari, V. Pavone, R. O. Louro and A. Lombardi, Chem. Commun., 2021, 57, 990 DOI: 10.1039/D0CC06676A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements