Experimental and Computational Study of the Monomer-Dimer Equilibrium in Dehaloperoxidase from Amphitrite Ornata
โ Scribed by Franzen, Stefan; de Serrano, Vesna; Oliver, Ryan C.; Krueger, Joanna
- Book ID
- 123126144
- Publisher
- Biophysical Society
- Year
- 2010
- Tongue
- English
- Weight
- 42 KB
- Volume
- 98
- Category
- Article
- ISSN
- 0006-3495
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๐ SIMILAR VOLUMES
The dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata is an enzyme that converts para-halogenated phenols to the corresponding quinones in the presence of hydrogen peroxide. Its enzymatic activity is similar to that of heme peroxidases such as horseradish peroxidase, yet it has
Non-empirical calculations on lithium and sodium gem-difluoroallyl and dlfhmromethyl systems show that the monomerdimer equilibrium is shifted in favour of the dimeric species. The two dlfluoromethyl systems show geometric and energetic features very close to those found in the larger systems. Diflu