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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Free Radic Biol Med. 2016 Oct 29;101:367–377. doi: 10.1016/j.freeradbiomed.2016.10.503

Figure 1.

Figure 1

Hydrogen-bonding among the “triad” of heme, BH4 and l-arg. This network of bonds rigidifies the heme pocket scaffolding and regulates the heme spin-state changes caused by water ligation to the Fe(III). The O2 bound to the heme is poised to attack the l-arg substrate. Adapted from the 1.85 Å resolution crystal structure of nNOSox, PDB: 2G6M.