The conduction of protons through human Nox2 has pre-viously been shown to be dependent upon His115. Align-ment of sequences for both animal and plant Nox proteins indicated that histidines 115 and 119 are both highly con-served, while His111 was conserved among animal homo-logues of Nox1–4. To investigate the possible role that these histidine residues might play in the conduction of protons through Nox2, we have introduced both paired and single mutations into these histidine residues. Each construct was used to generate a CHO cell line in which the expression of themutatedNox2was assessed
