1.14.14.47	Iron	in the presence of L-arginine and tetrahydrofolate, wild-type and mutants W66F and W66H exist in the typical Fe(III) high-spin configuration	
1.14.14.47	Iron	the enzyme's reductase domain utilizes a 2Fe2S cluster for electron transfer	
1.14.14.47	Iron	in the substrate-free form, the Fe-Cys stretching mode is detected at 342.5 per cm, similar to that of Bacillus subtilis NOS. The binding of L-Arg and N-hydroxy-L-arginine brings about a small decrease and increase in the Fe-Cys stretching frequency, respectively	
1.14.14.47	Iron	resonance Raman and ATR-FTIR spectroscopic study. The resting native ferric NOS exhibits an exclusive five-coordinate high-spin iron status. The nyFe-CO and nyCO mode frequencies indicate a weaker electrostatic interaction between Arg and CO. NOS is characterized by a stronger Fe-S bond, a lower ny4 frequency, and a negative shift in the nyFe-CO/nyCO correlation. The effects of tetrahydrobioptein on NOS heme structure are minor compared to the ones reported on the enzyme from Mus musculus