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. Author manuscript; available in PMC: 2008 Aug 1.
Published in final edited form as: Free Radic Biol Med. 2007 Apr 1;43(3):319–331. doi: 10.1016/j.freeradbiomed.2007.03.028

Fig. 1. Schematic Structure of Nox2 and p22phox.

Fig. 1

Indicated are Nox2 and p22phox, with predicted α-helical transmembrane regions depicted as cylinders, with the cytosol-facing B loop connecting helices 2 and 3, and hemes indicated in red, with conserved histidine residues in helices 3 and 5 providing axial and distal ligands to the heme irons (red circles). Helix 6 is connected to the predicted globular flavoprotein domain containing flavin adenine nucleotide (FAD) and the NADPH binding site, located on the cytosolic side. Nox2 is associated in the membrane with p22phox, which has 2 predicted α-helical transmembrane segments and whose C-terminus contains a proline-rich region (PRR) which is the target for binding by the bis-SH3 domain of p47phox.