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BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH L-ARG AND NO(H4B-FREE)
OverviewOverview
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.
About this StructureAbout this Structure
1FOO is a Single protein structure of sequence from Bos taurus with CAC, ACT, ZN, HEM, NO, ARG and GOL as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors., Li H, Raman CS, Martasek P, Masters BS, Poulos TL, Biochemistry. 2001 May 8;40(18):5399-406. PMID:11331003
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