Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors

Huiying Li, C. S. Raman, Pavel Martásek, Bettie Sue S. Masters, Thomas L. Poulos

Research output: Contribution to journalArticlepeer-review

73 Scopus citations

Abstract

The crystal structure of the endothelial nitric oxide synthase (NOS) heme domain complexed with NO reveals close hydrogen bonding interactions between NO and the terminal guanidino nitrogen of the substrate, L-arginine. Dioxygen is expected to bind in a similar mode which will facilitate proton abstraction from L-Arg to dioxygen, a required step for O-O bond cleavage. Structures of mechanism-based NOS inhibitors, N5-(1-iminoethyl)-L-ornithine and N-(3-(aminomethyl)benzyl)acetamidine, provide clues on how this class of compounds operate as suicide substrate inhibitors leading to heme oxidation.

Original languageEnglish (US)
Pages (from-to)5399-5406
Number of pages8
JournalBiochemistry
Volume40
Issue number18
DOIs
StatePublished - May 8 2001

ASJC Scopus subject areas

  • Biochemistry

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