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	719983	
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	740047	
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	740043	
1.14.14.47	Iron	the enzyme's reductase domain utilizes a 2Fe2S cluster for electron transfer	720895