AI Summary
The article discusses the potential of utilizing optimized radicals as novel catalysts in chemical reactions. Researchers are focusing on oxidases, enzymes that catalyze oxidation reactions, to replicate the efficiency of natural enzymes using inexpensive materials in laboratory settings. Specifically, the team at Humboldt University of Berlin has found a way to increase the oxidizing capacity of the phenoxyl radical found in galactose oxidase by binding it to iron, offering promising applications in research and industry.
Stronger than nature: Optimized radicals as potential novel catalysts
March 13, 2024
Nature uses enzymes for various metabolic processes. These biological catalysts are extremely efficient. Biomimetic catalysts based on inexpensive starting materials from the laboratory that can reproduce the efficiency of the natural enzymes and can function at ambient conditions are therefore of great interest to research and industry.
In a project led by the Institute of Chemistry at the Humboldt-Universität zu Berlin (HU), researchers have been investigating a special group of biological catalysts known as oxidases. These enzymes catalyze various oxidation reactions, where electrons are released from one substance and absorbed by another. Small, highly reactive particles, so-called radicals, often play an important role in these processes.
Oxidizing capacity improved by binding to iron
The enzyme of present interest is galactose oxidase found in many types of fungi, where a phenoxyl radical is used as the oxidant. The team led by HU researcher Kallol Ray has now found a way to utilize the phenoxyl radical in the laboratory in such a way that the oxidation capacity can be increased significantly.
In the naturally occurring enzyme, the phenoxyl radical is stabilized by a sulfur atom, which