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. 2020 Sep 8;9(9):839. doi: 10.3390/antiox9090839

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Xanthine oxidoreductase (XOR) structure and activities. Each XOR subunit is composed of three domains connected by unstructured regions (*) and characterized by: (i) two iron-sulfur redox centers (2Fe/S), (ii) a flavin adenine dinucleotide (FAD) cofactor and (iii) a molybdenum containing molybdopterin cofactor (Moco). The dotted arrows show the electron (e⁻) flux direction. The products and functions of each XOR activity are indicated: reduced nicotinamide adenine dinucleotide (NADH); nitric oxide (NO); reactive oxygen species (ROS); and uric acid (UA).