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- W2023553716 abstract "The nitric oxide synthase oxygenase domain (NOS ox ) oxidizes arginine to synthesize the cellular signal and defensive cytotoxin nitric oxide (NO). Crystal structures determined for cytokine-inducible NOS ox reveal an unusual fold and heme environment for stabilization of activated oxygen intermediates key for catalysis. A winged β sheet engenders a curved α-β domain resembling a baseball catcher's mitt with heme clasped in the palm. The location of exposed hydrophobic residues and the results of mutational analysis place the dimer interface adjacent to the heme-binding pocket. Juxtaposed hydrophobic O 2 - and polar l -arginine–binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis." @default.
- W2023553716 created "2016-06-24" @default.
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- W2023553716 date "1997-10-17" @default.
- W2023553716 modified "2023-10-15" @default.
- W2023553716 title "The Structure of Nitric Oxide Synthase Oxygenase Domain and Inhibitor Complexes" @default.
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- W2023553716 doi "https://doi.org/10.1126/science.278.5337.425" @default.
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