Metalloprotein–Inhibitor Binding: Human Carbonic Anhydrase II as a Model for Probing Metal–Ligand Interactions in a Metalloprotein Active Site
نویسندگان
چکیده
منابع مشابه
A short, strong hydrogen bond in the active site of human carbonic anhydrase II.
The crystal structure of human carbonic anhydrase II (HCA II) obtained at 0.9 A resolution reveals that a water molecule, termed deep water, Dw, and bound in a hydrophobic pocket of the active site forms a short, strong hydrogen bond with the zinc-bound solvent molecule, a conclusion based on the observed oxygen-oxygen distance of 2.45 A. This water structure has similarities with hydrated hydr...
متن کاملStructural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II.
In the catalysis of the hydration of carbon dioxide and dehydration of bicarbonate by human carbonic anhydrase II (HCA II), a histidine residue (His64) shuttles protons between the zinc-bound solvent molecule and the bulk solution. To evaluate the effect of the position of the shuttle histidine and pH on proton shuttling, we have examined the catalysis and crystal structures of wild-type HCA II...
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Enzymes catalyze many biological reactions. The rates of chemical reaction in the presence ofenzymes are, in some cases, accelerated more than 10 orders of magnitude relative to thecorresponding rates in solution.In this paper a comparison between optimized structures of two enzyme molecules in aspect ofenergy and dipole moment in different conditions including presence of metallic ion, without...
متن کاملStudy of Binding Interactions of Human Carbonic Anhydrase Xii
Objective: The present study was carried out to study the binding interactions of different N’-(substituted phenyl sulfonyl)-pyridine-2carbohydrazide derivatives and N’-(substituted phenyl sulfonyl)-thiophene-2-carbohydrazide derivatives which were synthesized by senior students from research laboratory, with objective to explore the suitability of selected ligands for their binding affinity fo...
متن کاملActive-site solvent replenishment observed during human carbonic anhydrase II catalysis
Human carbonic anhydrase II (hCA II) is a zinc metalloenzyme that catalyzes the reversible hydration/dehydration of CO2/HCO3-. Although hCA II has been extensively studied to investigate the proton-transfer process that occurs in the active site, its underlying mechanism is still not fully understood. Here, ultrahigh-resolution crystallographic structures of hCA II cryocooled under CO2 pressure...
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ژورنال
عنوان ژورنال: Inorganic Chemistry
سال: 2013
ISSN: 0020-1669,1520-510X
DOI: 10.1021/ic400295f