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 journalArticle

73 Citations (Scopus)

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

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Nitric Oxide Synthase Type III
Heme
Nitric Oxide
Oxygen
Corrosion inhibitors
Substrates
Hydrogen Bonding
Nitric Oxide Synthase
Suicide
Arginine
Protons
Hydrogen bonds
Nitrogen
Crystal structure
Oxidation
N(G)-iminoethylornithine
N-(3-(aminomethyl)benzyl)acetamidine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors. / Li, Huiying; Raman, C. S.; Martásek, Pavel; Masters, Bettie Sue S; Poulos, Thomas L.

In: Biochemistry, Vol. 40, No. 18, 08.05.2001, p. 5399-5406.

Research output: Contribution to journalArticle

Li, Huiying ; Raman, C. S. ; Martásek, Pavel ; Masters, Bettie Sue S ; Poulos, Thomas L. / Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors. In: Biochemistry. 2001 ; Vol. 40, No. 18. pp. 5399-5406.
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