Article
Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy.
The FEBS journal - 1 Feb 2022
Hofbauer Stefan, Pignataro Marcello, Borsari Marco, Bortolotti Carlo Augusto, Di Rocco Giulia, Ravenscroft Gianina, Furtmüller Paul G, Obinger Christian, Sola Marco, Battistuzzi Gianantonio
Abstract excerpt
The autosomal dominant striated muscle disease myoglobinopathy is due to the single point mutation His98Tyr in human myoglobin (MB), the heme protein responsible for binding, storage, and controlled release of O2 in striated muscle. In order to understand the molecular basis of this disease, a comprehensive biochemical and biophysical study on wt MB and the variant H98Y has been performed. Although only small...
Topics
- Histidine
- Humans
- Hydrogen Peroxide
- Models, Molecular
- Muscular Diseases
- Mutation
- Myoglobin
- Protein Conformation