@article{ref1,
title="Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors",
journal="Biochemistry",
year="2001",
author="Li, H. and Raman, C. S. and Martásek, P. and Masters, B. S. and Poulos, T. L.",
volume="40",
number="18",
pages="5399-5406",
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, 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>",
language="en",
issn="0006-2960",
doi="10.1021/bi002658v",
url="http://dx.doi.org/10.1021/bi002658v"
}