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A 2021 report described an engineered iron-based nanozyme that was 12 times as efficient as horseradish peroxidase (HRP) in a specific laboratory test. The comparison used tetramethylbenzidine (TMB) in a peroxidase assay under the same reaction conditions. It was not a general finding that the material is 12 times better in every setting, nor does the report establish a current world record.
What was the artificial enzyme?
It was an FeN3P-centred single-atom nanozyme: an engineered nanomaterial designed to imitate some of an enzyme’s catalytic behavior. It was not horseradish peroxidase extracted from a plant or a modified version of that natural enzyme. The research team, led by Yadong Li at Tsinghua University, built a carbon-and-nitrogen framework, added iron and phosphorus, then used pyrolysis to make a powder. Analyses reported iron, nitrogen and phosphorus atoms distributed in clusters through the carbon lattice.
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The design focused on the iron atoms’ local coordination environment—the nearby atoms and their arrangement. By controlling that structure, the researchers sought to tune the material’s catalytic activity. Team member Dingsheng Wang said, “More importantly, we demonstrate that the catalytic performance can be modulated via local structure control of active sites and their coordination environment.”
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In the reported peroxidase assay, the nanozyme acted on TMB under the same reaction conditions as HRP. Chemistry World reported in 2021 that the material was “12 times more efficient” than HRP in that comparison. The claim applies to that assay and its conditions—not to every substrate, reaction, or use of the material.
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A fold comparison is only meaningful alongside its measurement basis. Nanozyme activity can be expressed per active site, particle, or mass, and those choices can produce different-looking comparisons. Conditions and how catalyst concentration or active sites are counted also matter. The 12-times figure should therefore be read as the study’s specific TMB peroxidase result, not as a universal multiplier for artificial enzymes.
Was this a record, and does it still hold?
The 2021 report presented the result as a record at that time. That dated description is not enough to establish that the FeN3P material remains the highest-performing nanozyme today. Later work includes different materials and activity measures, and the available evidence does not provide an apples-to-apples ranking across them. A present-day record claim would require comparable assays, conditions and activity calculations.
What happened in the mouse experiment?
The researchers also injected the nanozyme into tumours in living mice. Fourteen days later, the treated tumours were reported to be less than half the size of tumours in untreated controls. The report said no toxic effects were observed in that experiment.
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Those results are from an animal study. They do not demonstrate that the material treats cancer in people, establish human safety, or show that it is an approved or available treatment. An observation of no toxicity in one reported experiment is not proof of safety in humans.
Has it been tested in people or made into a treatment?
The 2021 paper and reporting establish laboratory and preclinical findings, not human trial results. They do not establish regulatory approval, a marketed therapeutic or diagnostic product, or commercial availability of this specific FeN3P nanozyme. The mouse findings should not be interpreted as medical advice or a reason to delay established cancer care.
Independent reader supportYour contribution helps us test, update, and keep practical guides available for everyone.Why does the comparison matter?
HRP is a natural enzyme used as a comparator in the TMB peroxidase assay. The result illustrates how engineering the local structure around single iron atoms in a carbon-based framework can produce catalytic activity that, in that particular test, exceeded HRP’s. It is a materials-science finding—not evidence that the nanozyme is broadly superior to natural enzymes or ready for clinical use.
Vince Rotello, an artificial-enzyme researcher at the University of Massachusetts, said: “Nature uses exquisite control over metal ligation to provide highly efficient catalysts. This structural control is elegantly modelled here in single-metal catalysts.” He added: “The single-atom strategy presented is a promising direction for the creation of nanocatalysts for biological, environmental and chemical applications.”
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