@article{NishinoOkamotoLeimkuehler2017,
  author    = {Nishino, Takeshi and Okamoto, Ken and Leimk{\"u}hler, Silke},
  title     = {Enzymes of the Xanthine Oxidase Family},
  series = {Molybdenum and tungsten enzymes : biochemistry},
  volume    = {5},
  journal   = {Molybdenum and tungsten enzymes : biochemistry},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  isbn      = {978-1-78262-391-5},
  doi       = {10.1039/9781782623915-00192},
  pages     = {192 -- 239},
  year      = {2017},
  abstract  = {Enzymes from the xanthine oxidase (XO) family of molybdenum enzymes are generally, with some exceptions, molybdenum iron-sulfur flavin hydroxylases. Mammalian xanthine oxidoreductase and aldehyde oxidase were among the first enzymes to be studied in detail more than 100 years ago and, surprisingly, they continue to be thoroughly studied in molecular detail with many open and unresolved questions remaining. Enzymes of the XO family are characterized by a molybdenum cofactor (Moco) active site with a MoVIOS(OH) ligand sphere where substrate hydroxylation of either aromatic or aliphatic carbon centers is catalyzed. During the reaction, electrons are transferred to the oxidizing substrate, most commonly O2 or NAD+, which react at the FAD site.},
  language  = {en}
}