Triplet Acetone Generation by Pseudoperoxidase Activity of Myoglobin: Structural Damage and Quenching
Thiago M V Gomes, Cassius V Stevani, Kostas Pantopoulos, Luiz D Ramos, Etelvino J H Bechara · 2026
Read Triplet Acetone Generation by Pseudoperoxidase Activity of Myoglobin: Structural Damage and Quenching by Thiago M V Gomes, Cassius V Stevani, Kostas Pantopoulos, Luiz D Ramos, Etelvino J H Bechara (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13556174.txt.
Description
Excited molecules in a high-energy triplet state can damage living tissue, and Thiago Gomes and co-authors catch one being made by a familiar protein in a 2026 study. Myoglobin, the oxygen store in muscle, can act like a weak peroxidase enzyme. Fed a small aldehyde, it produced triplet-state acetone, a reactive excited molecule.
The team proved the claim several ways: the protein's color band shifted during the reaction, faint light was emitted, a probe dye brightened that emission, and known quenchers dimmed it. Oxygen use followed clean first-order behavior. The reaction also scarred the myoglobin itself. The finding matters because broken muscle spills myoglobin into the blood, a state called rhabdomyolysis, where such chemistry could add injury. The authors compare the system with a classic plant enzyme reaction.
Catalog record
| CREATOR | Thiago M V Gomes, Cassius V Stevani, Kostas Pantopoulos, Luiz D Ramos, Etelvino J H Bechara |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 33 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |