A number of previous studies have determined that a metalloenzyme active site is inherently determined by the ligands and metal and only weakly perturbed by the surrounding protein environment. This conclusion is now being tested for several families of bimetallic enzymes. Metal substitution is exam
Ab Initio Structure of the Active Site of Phosphotriesterase
โ Scribed by Krauss, M.
- Book ID
- 127322249
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 534 KB
- Volume
- 41
- Category
- Article
- ISSN
- 0095-2338
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๐ SIMILAR VOLUMES
Possible structures of the active site of a metalloglutathione transferase ลฝ . enzyme FosA are deduced from ab initio calculations. The active site of the manganese ลฝ . fosfomycin resistance protein FosA was reported, from electron paramagnetic resonance ลฝ . EPR studies, to have three waters bound i
Ab initio molecular orbital calcuiations using a contracted basis of gaussian orbitals on the system methanethiol/imidazole are reported. For the hydrogen bond S---H---N in this system, which was chosen as a mode1 for the active site of papain, a double-well potential was found at a S-N separation o