Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua.
Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua.
复制标题
来自无害李斯特菌的新型铁蛋白的铁氧化和水解反应。
DOI:
10.1042/bj3490783
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发表时间:
2000
期刊:
影响因子:
--
通讯作者:
Chasteen,ND
中科院分区:
文献类型:
--
作者:
Yang,X;Chiancone,E;Stefanini,S;Ilari,A;Chasteen,ND
Iron deposition in the unusual 12-subunit ferritin from the bacteriumListeria innocuaproceeds in three phases: a rapid first phase in which Fe2+binds to the apoprotein, PZof chargeZ, according to the postulated reaction 2Fe2++PZ→ [Fe2–P]Z+2+2H+, where [Fe2–P]Z+2represents a dinuclear iron(II) complex formed at each of the 12 ferroxidase centres of the protein; a second phase corresponding to oxidation of this putative complex, i.e. [Fe2–P]Z+2+½O2→ [Fe2O–P]Z+2H+; and a third phase of iron(II) oxidation/mineralization, i.e. 4Fe2++O2+8H2O → 8FeOOH(s)+8H+[where FeOOH(s)represents the hydrous ferric oxide mineral that precipitates from the solution], which occurs when iron is added in excess of 24Fe2+/protein. In contrast with other ferritins, the ferroxidation reaction inL. innocuaferritin proceeds more slowly than the oxidation/mineralization reaction. Water is the final product of dioxygen reduction in the 12-subunitL. innocuaferritin (the present work) and in the 24-subunitEscherichia colibacterioferritin, whereas H2O2is produced in 24-subunit mammalian ferritins. Possible reasons for this difference are discussed.