Issue 36, 2023

A macrocyclic quinol-containing ligand enables high catalase activity even with a redox-inactive metal at the expense of the ability to mimic superoxide dismutase

Abstract

Previously, we found that linear quinol-containing ligands could allow manganese complexes to act as functional mimics of superoxide dismutase (SOD). The redox activity of the quinol enables even Zn(II) complexes with these ligands to catalyze superoxide degradation. As we were investigating the abilities of manganese and iron complexes with 1,8-bis(2,5-dihydroxybenzyl)-1,4,8,11-tetraazacyclotetradecane (H4qp4) to act as redox-responsive contrast agents for magnetic resonance imaging (MRI), we found evidence that they could also catalyze the dismutation of H2O2. Here, we investigate the antioxidant behavior of Mn(II), Fe(II), and Zn(II) complexes with H4qp4. Although the H4qp4 complexes are relatively poor mimetics of SOD, with only the manganese complex displaying above-baseline catalysis, all three display extremely potent catalase activity. The ability of the Zn(II) complex to catalyze the degradation of H2O2 demonstrates that the use of a redox-active ligand can enable redox-inactive metals to catalyze the decomposition of reactive oxygen species (ROS) besides superoxide. The results also demonstrate that the ligand framework can tune antioxidant activity towards specific ROS.

Graphical abstract: A macrocyclic quinol-containing ligand enables high catalase activity even with a redox-inactive metal at the expense of the ability to mimic superoxide dismutase

Supplementary files

Article information

Article type
Edge Article
Submitted
10 mai 2023
Accepted
25 ago 2023
First published
05 set 2023
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2023,14, 9910-9922

A macrocyclic quinol-containing ligand enables high catalase activity even with a redox-inactive metal at the expense of the ability to mimic superoxide dismutase

S. Karbalaei, A. Franke, J. Oppelt, T. Aziz, A. Jordan, P. R. Pokkuluri, D. D. Schwartz, I. Ivanović-Burmazović and C. R. Goldsmith, Chem. Sci., 2023, 14, 9910 DOI: 10.1039/D3SC02398B

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements