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
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
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.