Alcohol dehydrogenase from the hyperthermophilic archaeon Pyrobaculum aerophilum: Stability at high temperature
2012
Abstract The structural and stability properties of a novel zinc-dependent alcohol dehydrogenase from the hyperthermophilic archaeon Pyrobaculum aerophilum (PyAeADHII) were investigated by Fourier transformed infrared spectroscopy (FTIR). This enzyme is a thermostable homo-tetramer belonging to the GroES-fold motif proteins characterized by an irregular β-barrel conformation. Our results revealed a protein with a secondary structure rich in β-sheet (32% of the total secondary elements) and it showed a three-step thermal unfolding pathway. The complete enzyme denaturation was preceded by the formation of a relaxed tertiary/quaternary structure and previously by an excited native-like conformation. Two-dimensional correlation spectroscopy analysis (2D-COS) and differential scanning calorimetry (DSC) experiments supported these data and allowed us to determine the protein melting temperature at 96.9 °C as well as to suggest the sequence of the events that occurred during the protein denaturation process.
Keywords:
- Enzyme
- Protein quaternary structure
- Denaturation (biochemistry)
- Molecular biology
- Differential scanning calorimetry
- Protein secondary structure
- Crystallography
- Biochemistry
- Infrared spectroscopy
- Two-dimensional nuclear magnetic resonance spectroscopy
- Chemistry
- Alcohol dehydrogenase
- Fourier transform infrared spectroscopy
- Correction
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