%0 Journal Article
%T Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors
%J Biochemistry
%D 2001
%A Li, H.
%A Raman, C. S.
%A Martásek, P.
%A Masters, B. S.
%A Poulos, T. L.
%V 40
%N 18
%P 5399-5406
%X 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, N(5)-(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.<p /><p>Language: en</p>
%G en
%I American Chemical Society
%@ 0006-2960
%U http://dx.doi.org/10.1021/bi002658v