Binding of intermediate, product, and substrate analogs to neuronal nitric oxide synthase: Ferriheme is sensitive to ligand-specific effects in the L-arginine binding site

John C. Salerno, Kirk McMillan, Bettle Sue Siler Masters

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

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(w)-hydroxy-L-arginine, N(w)-methyl-L-arginine, and N(w)-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.

Original languageEnglish (US)
Pages (from-to)11839-11845
Number of pages7
JournalBiochemistry
Volume35
Issue number36
DOIs
StatePublished - 1996

ASJC Scopus subject areas

  • Biochemistry

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