Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: Binding of ligands at the arginine site induces changes in the heme ligation geometry

John C. Salerno, Pavel Martasek, Linda J. Roman, Bettie Sue S. Masters

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

The electron paramagnetic resonance spectra of the heme domain of inducible nitric oxide synthase (iNOS) demonstrate a close relationship to the corresponding spectra of the neuronal isoform (nNOS). The binding of ligands to the iNOS arginine site perturbs the environment of the high spin ferriheme in a highly ligand-specific manner. The iNOS forms five-coordinate, high-spin complexes with arginine analogs which are clearly related to the corresponding complexes of nNOS. Studies indicate that the binding of L- arginine, N(ω)-hydroxy-L-arginine (NHA), and N(ω)-methyl-L-arginine (NMA) produces various spectroscopic species closely corresponding to the equivalent complexes of nNOS, while N(ω)-nitro-L-arginine (NNA) binding produces a state which appears intermediate in character between the nNOS NNA and arginine complexes. These spectroscopic studies have permitted the determination of ligand-specific high-spin states which reveal similarities and differences between iNOS and nNOS.

Original languageEnglish (US)
Pages (from-to)7626-7630
Number of pages5
JournalBiochemistry
Volume35
Issue number24
DOIs
StatePublished - Jun 18 1996

ASJC Scopus subject areas

  • Biochemistry

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