Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.2.7.5 extracted from

  • Sugimoto, H.; Tano, H.; Tajima, R.; Miyake, H.; Tsukube, H.; Ohi, H.; Itoh, S.
    In situ generation of oxo-sulfidobis(dithiolene)tungsten(VI) complexes: active-site models for the aldehyde ferredoxin oxidoreductase family of tungsten enzymes (2007), Inorg. Chem., 46, 8460-8462.
    View publication on PubMed

Application

Application Comment Organism
analysis in situ generation of oxo-sulfidobis(dithiolene)tungsten(VI) complexes that model the proposed active-site structure for the AOR family of tungsten enzymes. The complexes are characterized by UV-vis, electrospray ionization mass spectrometry, IR, and resonance Raman spectroscopies and are found to mimic the coordination environment including the W=E (E=O, S) bond strengths and hydrolytic reactions of the tungsten center of the AOR family synthetic construct

Organism

Organism UniProt Comment Textmining
synthetic construct
-
-
-

Synonyms

Synonyms Comment Organism
AOR
-
synthetic construct

Cofactor

Cofactor Comment Organism Structure
additional information the active tungsten center is hydrolyzed to the inactive dioxotungsten(VI) center ([WVIO2]2+) in the absence of sulfide synthetic construct