1.14.13.39 Ca2+ - 440191, 440194, 440203, 440205, 440210, 440234, 440236, 659646, 671631, 675257, 686010 1.14.13.39 Ca2+ absolutely dependent on 440215, 440227 1.14.13.39 Ca2+ activates 684277 1.14.13.39 Ca2+ activates both isozymes 687358 1.14.13.39 Ca2+ activation only in the presence of calmodulin 440211, 440214 1.14.13.39 Ca2+ Ca2+/calmodulin is required for citrulline/NO formation and for superoxide formation in absence of tetrahydropterin 440218 1.14.13.39 Ca2+ cerebellum enzyme is Ca2+-dependent 440202, 440232 1.14.13.39 Ca2+ constitutive endothelial and inducible membrane bound macrophage enzyme are strictly Ca2+-dependent 440204 1.14.13.39 Ca2+ dependent on 685094, 687697 1.14.13.39 Ca2+ dependent, NOS1 and NOS3 701646 1.14.13.39 Ca2+ insoluble enzyme 440204 1.14.13.39 Ca2+ low levels of Ca2+ stimulate nNOS activity 699996 1.14.13.39 Ca2+ macrophage enzyme 440204 1.14.13.39 Ca2+ no stimulation with exogenous Ca2+, inducible isoform from liver 440237 1.14.13.39 Ca2+ required 440228, 440230, 440231, 440235, 440240, 658405, 658767, 685095, 763831, 764203, 765745 1.14.13.39 Ca2+ required by eNOS, activates 687615 1.14.13.39 Ca2+ required for calmodulin to bind and activate the enzyme, maximum calmodulin-dependent activity is measured at 1.5 mM CaCl2 696280 1.14.13.39 Ca2+ required for catalysis 687291 1.14.13.39 Ca2+ required, calmodulin independent 440208, 440224 1.14.13.39 Ca2+ requirement, brain, not liver or lung 440190 1.14.13.39 Ca2+ retina enzyme is dependent on Ca2+ 440232 1.14.13.39 Ca2+ slight activation 440201 1.14.13.39 Ca2+ stimulation of mtNOS can be achieved by elevating mitochondrial Ca2+ (0.01-0.1 mM) 699997 1.14.13.39 Ca2+ the enzyme bears Ca2+/calmodulin dependent cytochrome P-450 reductase activity which catalyzes cytochrome c reduction 440199 1.14.13.39 Ca2+ the raise of intracellular calcium levels increases nNOS dephosphorylation and enzymatic activity 700432 1.14.13.39 Ca2+/calmodulin activate the electron transfer 673804 1.14.13.39 Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme 674558 1.14.13.39 Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme 674558 1.14.13.39 Fe2+ - 671728, 686010 1.14.13.39 Fe2+ a cytochrome P450 enzyme 687615 1.14.13.39 Fe2+ a heme enzyme 685094, 687579, 687697 1.14.13.39 Fe2+ a heme enzyme, frequencies of electron transfer, overview 687572 1.14.13.39 Fe2+ a heme enzyme, spectral comparison of the FeIII-NO and FeII-NO complexes of the bacterial NOSs, FeIII-NO complexes lack change in Fe-N-O frequencies upon (6R) 5,6,7,8-tetrahydro-L-biopterin binding to bacterial NOSs, overview. In the FeIII-NO complexes, both L-arginine and NOHA induced the Fe-N-O bending mode at nearly the same frequency as a result of a steric interaction between the substrates and the heme-bound NO, while in FeII-NO complexes the the Fe-N-O bending mode is no observed 684957 1.14.13.39 Fe2+ in heme 765779 1.14.13.39 Fe2+ in the heme 763831, 764203, 765745 1.14.13.39 Fe2+ in the heme cofactor 685120 1.14.13.39 Fe2+ in the heme cofactor, substrate-ligand interaction in the Fe2+-O2 complex, overview 687291 1.14.13.39 Fe2+ required 685095 1.14.13.39 Iron - 440218, 440220 1.14.13.39 Iron 0.8 mol per mol of subunit 440216 1.14.13.39 Iron 0.83 mol per mol of subunit 440238 1.14.13.39 Iron 0.88 mol per mol of recombinant enzyme monomer 440233 1.14.13.39 Iron 0.9-1.2 mol heme per mol of dimer 440223 1.14.13.39 Iron 2 mol iron-protoporphyrin IX per mol enzyme dimer, the heme-iron is ferric, EPR-and light absorbance spectroscopy 440192 1.14.13.39 Iron as heme iron in protoporphyrin IX /heme, heme–substrate interactions and heme-transitions, overview 671709 1.14.13.39 Iron ferric heme 659257 1.14.13.39 Iron heme 659330 1.14.13.39 Iron heme iron 672016 1.14.13.39 Iron heme iron, FMN/heme electron transfer 674558 1.14.13.39 Iron heme ligand is bound via C415 440234 1.14.13.39 Iron heme-iron 440216, 440221, 440223, 440240 1.14.13.39 Iron low-spin heme iron, L-arginine and tetrahydrobiopterin bind and stabilize heme iron in five-coordinate high-spin state 658119 1.14.13.39 Iron low-spin heme iron, L-arginine aud tetrahydrobiopterin bind and stabilize heme iron in five-coordinate high-spin state 658119 1.14.13.39 Iron mouse macrophage enzyme: cytochrome P-450 type hemoprotein 440198 1.14.13.39 Iron naturally occuring neuronal mutant with a 105-amino acid deletion in the heme-binding domain as a result of in-frame mutation by specific alternative splicing, contains heme, but shows no L-arginine and NADPH-dependent citrulline-forming activity in presence of Ca2+-promoted calmodulin, the heme coordination geometry is highly abnormal 440217 1.14.13.39 Iron protoporphyrin IX heme 440198, 440222, 440223, 440225, 440238 1.14.13.39 Iron required 440223 1.14.13.39 Mg2+ activates both isozymes 687358 1.14.13.39 O2 oxygen tension influences the activity 673804 1.14.13.39 Zinc 0.43 mol per mol of subunit 440216 1.14.13.39 Zn2+ bound by Cys104, Cys109, and Cys194 of isozyme iNOS oxygenase domain 674558