Modeling of active site of cytochrome P-450IA2
✍ Scribed by E. Lopez-de-Briñas; F. Manaut; F. Sanz; J.J. Lozano; E. Lozoya
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 427 KB
- Volume
- 12
- Category
- Article
- ISSN
- 0263-7855
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The vaccinia virus cDNA expression system was used t o produce human cytochrome P450 IA2 in a hepatoma cell line that is devoid o f significant basal levels o f P450. The expressed enzyme yielded a reduced carbon monoxide-bound difference spectrum with a A , , , of 449 nm. Catalytic activities and m
Hydration of protein cavities influences protein stability, dynamics, and function. Protein active sites usually contain water molecules that, upon ligand binding, are either displaced into bulk solvent or retained to mediate protein-ligand interactions. The contribution of water molecules to ligand
The oxidation of uroporphyrinogen, an intermediate of the heme biosynthetic pathway, by methylcholanthrene-inducible isozyme(s) of cytochrome P-450 has been proposed to play a role in the development of chemically induced uroporphyria. Prior work from this laboratory [lo] indicated that although add
## Abstract QM/MM calculations provide a means for predicting the electronic structure of the metal center in metalloproteins. Two heme peroxidases, Cytochrome __c__ Peroxidase (CcP) and Ascorbate Peroxidase (APX), have a structurally very similar active site, yet have active intermediates with ver