The inhibition of α-carbonic anhydrase (CA) enzyme by cyanate ion with five-fold ligand: A DFT study
Publish place: 21th Iranian Inorganic Chemistry Conference
Publish Year: 1398
نوع سند: مقاله کنفرانسی
زبان: English
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شناسه ملی سند علمی:
IICC21_181
تاریخ نمایه سازی: 5 آذر 1398
Abstract:
Density functional theory (DFT) using B3LYP functional and split-valance 6-311G** basis set have been employed tooptimized the geometry ofcyanate ion (OCN¯)inhibitor and complex between this inhibitor with active site of α-carbonic anhydrase (CA) enzyme. The results show that the zinc cation in the active site of the CA enzyme prefers tetrahedral geometry. While the cyanate anion is coordinated to the zinc, the geometry could be change to trigonal bipyramidal or the tetrahedral geometry [1,2],( Figure 1).It is noteworthy that among the anions studied as inhibitors, including: N3¯, SCN¯, HS¯, HSO3¯, CN , cyanateion performs the best inhibitor.Also the cyanateanion belongs the second group of inhibitors of α-carbonic anhydrase which possess pharmacological applications.
Authors
Mina Ghiasi
Department of Chemistry, Faculty of Physics & Chemistry, Alzahra University, ۱۹۸۳۵-۳۸۹, Vanak, Tehran, Iran.
Azar Larijani
Department of Chemistry, Faculty of Physics & Chemistry, Alzahra University, ۱۹۸۳۵-۳۸۹, Vanak, Tehran, Iran.