A COMPARISON BETWEEN THE STRUCTURES OF TUNGSTOPTERIN COFACTOR IN TUNGSTEN OXIDOREDUCTASE AND A MODEL COMPLEX, IS-DIOXOBIS(2,3-NAPHTHALENEDITHIOLATE)TUNGSTEN(VI) IN THEIR O-ATOM TRANSFER-REACTION

Citation
H. Oku et al., A COMPARISON BETWEEN THE STRUCTURES OF TUNGSTOPTERIN COFACTOR IN TUNGSTEN OXIDOREDUCTASE AND A MODEL COMPLEX, IS-DIOXOBIS(2,3-NAPHTHALENEDITHIOLATE)TUNGSTEN(VI) IN THEIR O-ATOM TRANSFER-REACTION, Chemistry Letters, (1), 1996, pp. 31-32
Citations number
12
Categorie Soggetti
Chemistry
Journal title
ISSN journal
03667022
Issue
1
Year of publication
1996
Pages
31 - 32
Database
ISI
SICI code
0366-7022(1996):1<31:ACBTSO>2.0.ZU;2-F
Abstract
In our study on an active site model of tungsten oxidoreductase, struc tural parameters of oxo and thiolate ligands in (NEt(4))(2)[(WO2)-O-VI (S2C10H6)(2)]. H2O (1) (S2C10H6 = 2,3-naphthalenedithiolato) were obta ined where two dithiolene like coordination exists. A comparison of th e structure with the enzyme active site indicated the importance of '' least stereochemical movement'' of thiolate ligands.