1.14.14.47	E25A/E26A/E316A	mutant facilitates crystallization	-, 740066	
1.14.14.47	E25A/E26A/E316A/Y357F	mutant facilitates crystallization	-, 740066	
1.14.14.47	I208V	crystallization and inhibition data	-, 740084	
1.14.14.47	L356R	mutation Lys-356 (Bacillus subtilis NOS) to Arg-365 (gsNOS) substitution alters the conformation of a conserved Asp carboxylate, resulting in movement of an Ile residue toward the heme	740683	
1.14.14.47	additional information	a chimera between enzyme and flavodoxin YkuN is 8fold more active tan wild-type. Adding excess amounts of YkuN does not significantly alter activity	-, 740728	
1.14.14.47	additional information	the proximal hydrogen bond modulation at residue W66 can selectively decrease or increase the electron donating properties of the proximal thiolate. The modulation controls the sigma-competition between distal and proximal ligands and controls the stability of various NOS intermediates. A fine tuning of the electron donation by the proximal ligand is required to allow at the same time oxygen activation and to prevent uncoupling reactions	-, 740692	
1.14.14.47	P332G	mutation at the center of the dimer interface, mutant displays significantly more monomer content than wild-type	-, 740863	
1.14.14.47	P332G/A333S	mutation at the center of the dimer interface, both mutations are necessary to mimic interactions at the dimer interface displayed by the mouse enzyme	-, 740863	
1.14.14.47	W66F	mutation changes midpoint potential from -361 mV for wild-type to -427 mV. Mutant displays 2.5fold lower activity when reaction is supported by flavoproteins or NADPH instead of tetrahydrofolate	719983	
1.14.14.47	W66F	mutation modulates hydrogen bond interaction to the thiolate ligand which controls the stability of various NOS intermediates	-, 740692