Chaoqun Wu

TL;DR: Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, the substrate L-arginine (L-Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and L-Arg binding complete the catalytic center for synthesis of the essential biological signal and cytotoxin nitricoxide.

TL;DR: Juxtaposed hydrophobic O2- and polar L-arginine-binding sites occupied by imidazole and aminoguanidine, respectively, provide a template for designing dual-function inhibitors and imply substrate-assisted catalysis.

TL;DR: It is proposed that cav-1 binding to eNOS reductase compromises its ability to bind CaM and to donate electrons to the eN OS heme, thereby inhibiting NO synthesis.

TL;DR: Results suggest that residues 66-114 of iNOSox are involved in productive H4biopterin interaction and subunit dimerization, and appears to stabilize the protein structure in this region, and through doing so activates iN OS for NO synthesis.

TL;DR: In this paper, pterin-free inducible NOS (iNOS) and iNOS reconstituted with eight different tetrahydro- or dihydropterins were investigated.