Arginine-Based Inhibitors of Nitric Oxide Synthase: Therapeutic Potential and Challenges
Figure 1
(a) Scheme of the two-step oxygenation of arginine catalysed by NO synthase. (b) Scheme of the mature NOS dimer: Each subunit contains tetrahydrobiopterin (BH4) and heme near the active site of the oxygenase domain (grey). The reductase domain (white) houses the NADPH-binding site as well as two-electron transfer cofactors (flavine adenine dinucleotide FAD and flavine mononucleotide FMN). The zinc bound at the interface mediates dimerisation. Calmodulin (CAM) binding regulates the activity.
