Mobilization of iron from ferritin by xanthine oxidase was studied under aerobic and anaerobic conditions. Aerobic iron release amounted to approx. 3.7 nmol/ml in 10 min. This amount was decreased by approx. 30% under anaerobic conditions. Aerobic iron mobilization involved two mechanisms. About 70% was released by O2.- generated by xanthine oxidase. The rest was released by O2(.-)-independent mechanisms, which also accounted for the total iron release when O2 was absent. A possible transfer of reducing equivalents directly from xanthine oxidase to ferritin is discussed. The results imply that, in pathological conditions with increased formation of O2.-, iron may be released from ferritin. Furthermore, in hypoxic tissues xanthine oxidase can release iron from ferritin by an O2(.-)-independent process. Free iron is liable to catalyse the formation of the extremely reactive and damaging OH. radical.
Research Article| April 01 1987
Release of iron from ferritin by xanthine oxidase. Role of the superoxide radical
Biochem J (1987) 243 (1): 55–59.
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B J Bolann, R J Ulvik; Release of iron from ferritin by xanthine oxidase. Role of the superoxide radical. Biochem J 1 April 1987; 243 (1): 55–59. doi: https://doi.org/10.1042/bj2430055
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