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Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea,...
The novel covalent conjugates 1 and 2 of porphyrins and tetraaza macrotricycles have been prepared. The compounds dissolve freely in aqueous buffer at neutral pH and bind nucleotides with good affinity, but insignificant selectivity. Heterodimer formation with porphyrin carboxylic anions was detected in the gas phase corroborating the prediction of forcefield calculations
Nitric oxide, a key signaling molecule, is produced by a family of enzymes collectively called nitric oxide synthases (NOS). Here, we report the crystal structure of the heme domain of endothelial NOS in tetrahydrobiopterin (H 4 B)-free and -bound forms at 1.95 Å and 1.9 Å resolution, respectively. In both structures a zinc ion is tetrahedrally coordinated to pairs of symmetry-related cysteine...
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