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- W1972822508 abstract "The electron paramagnetic resonance spectra of purified neuronal nitric oxide synthase indicates that the binding of ligands to the arginine site perturbs the environment of the high-spin ferriheme in a highly ligand-specific manner. Four categories of high-spin complex can be distinguished; all are five-coordinate, and all retain the axial thiolate ligand, but they differ in their ligation geometries. These spectroscopic species reveal distinct local conformations which can be stabilized individually by the binding of L-arginine, N omega-hydroxy-L-arginine, N omega-methyl-L-arginine, and N omega-nitro-L-arginine. Other arginine analog inhibitors stabilize one or more of these states, revealing patterns based on the nature of substituents at the terminal amino group." @default.
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- W1972822508 date "1996-01-01" @default.
- W1972822508 modified "2023-09-27" @default.
- W1972822508 title "Binding of Intermediate, Product, and Substrate Analogs to Neuronal Nitric Oxide Synthase: Ferriheme is Sensitive to Ligand-Specific Effects in the <scp>l</scp>-Arginine Binding Site" @default.
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- W1972822508 doi "https://doi.org/10.1021/bi953015w" @default.
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