Abstract
Nitric oxide synthases (NOS) are homodimeric enzymes which catalyze Arg to nitric oxide and citrulline (1). Its subunits contain a N-terminal oxygenase domain which can bind Fe-protoporphyrin IX (heme), Arg, and the essential cofactor 6R-tetrahydrobiopterin (H4B) and a C-terminal reductase domain containing binding sites for FAD, FMN, and NADPH.
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Wang, ZQ., Wei, CC., Santolini, J., Stuehr, D.J. (2002). Mutation of W457 Alters N-Hydroxy-L-Arginine Oxidation by Inducible no Synthase: A Single Turnover Study. In: Milstien, S., Kapatos, G., Levine, R.A., Shane, B. (eds) Chemistry and Biology of Pteridines and Folates. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0945-5_22
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DOI: https://doi.org/10.1007/978-1-4615-0945-5_22
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