Natural mutations of human XDH promote the nitrite (NO₂^-)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health?

6 B) with a slight trend for elevation with Asn909Lys and also Ile703Val at baseline and in the presence of reducing substrate confirming a general trend for increase with all of the mutations despite clear differences in the O 2 ·- generating activities of these mutations ( Fig. 6 C and D).

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Of note, febuxostat caused an elevation of O 2 ·- generation in the presence of both these substrates although this did not reach statistical significance.

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