Xanthine dehydrogenase (EC 1.1.1.204) is a molybdenum iron-sulfur, fla
vin hydroxylase whose physiological role is ascribed to purine catabol
ism. Its ready conversion to its oxidase counterpart, xanthine oxidase
(EC 1.1.3.22), under normal isolation conditions has complicated stud
ies of this enzyme in the past. Many studies in the past have looked a
t the role of xanthine oxidase in the metabolism of chemotherapeutic a
gents requiring bioreductive activation for their antineoplastic activ
ities. This paper reviews some of xanthine dehydrogenase's biological
and physiological parameters as well as recent studies into the xanthi
ne dehydrogenase-induced activation of bioreductive agents. Studies ar
e also presented that point out this enzyme's potential role in mitomy
cin C-induced cytotoxicity to EMT6 cells under aerobic and hypoxic con
ditions. The potential importance of xanthine dehydrogenase as an enzy
me targeted in chemotherapeutic regimens is discussed.