Is hydrogen peroxide produced during iron(II) oxidation in mammalian apoferritins

作者: Guanghua Zhao , Fadi Bou-Abdallah , Xiaoke Yang , Paolo Arosio , N. Dennis Chasteen

DOI: 10.1021/BI011052J

关键词: FerritinRecombinant DNACatalaseReagentCatalysisHydrogen peroxideStereochemistryCeruloplasminBiochemistryChemistryProtein subunit

摘要: The ferritins are a class of iron storage and detoxification proteins that play central role in the biological management iron. These have catalytic site, "the ferroxidase site", located on H-type subunit facilitates oxidation Fe(II) to Fe(III) by O(2). Measurements during past 10 years number vertebrate provided evidence H(2)O(2) is produced at this diiron site. Recently reported experiments using three different analytical methods with horse spleen ferritin (HoSF) failed detect production protein [Lindsay, S., Brosnahan, D., Watt, G. D. (2001) Biochemistry 40, 3340-3347]. findings contrast earlier results reporting HoSF [Xu, B., Chasteen, N. (1991) J. Biol. Chem. 266, 19965-19970]. Here sensitive fluorescence assay an based O(2) evolution presence catalase were used demonstrate as previously reported. However, because relatively few H-chain sites reaction protein, more difficult than recombinant human (HuHF). proper sequence addition reagents important for measurement total amount ferroxidation reaction.

参考文章(15)
Jean-Marie Lehn, JL Atwood, JED Davies, DD MacNicol, F Vögtle, Comprehensive Supramolecular Chemistry ,(1996)
M.D. Percival, Human 5-lipoxygenase contains an essential iron. Journal of Biological Chemistry. ,vol. 266, pp. 10058- 10061 ,(1991) , 10.1016/S0021-9258(18)99187-8
J.K. Grady, Y Chen, N.D. Chasteen, D.C. Harris, Hydroxyl radical production during oxidative deposition of iron in ferritin. Journal of Biological Chemistry. ,vol. 264, pp. 20224- 20229 ,(1989) , 10.1016/S0021-9258(19)47050-6
Xiaoke YANG, Emilia CHIANCONE, Simonetta STEFANINI, Andrea ILARI, Dennis N. CHASTEEN, Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua. Biochemical Journal. ,vol. 349, pp. 783- 786 ,(2000) , 10.1042/BJ3490783
J. Fetter, Jonathan Cohen, D. Danger, Joann Sanders-Loehr, E. C. Theil, The influence of conserved tyrosine 30 and tissue-dependent differences in sequence on ferritin function: use of blue and purple Fe(III) species as reporters of ferroxidation Journal of Biological Inorganic Chemistry. ,vol. 2, pp. 652- 661 ,(1997) , 10.1007/S007750050180
Michel Heusterspreute, Robert R. Crichton, Amino-acid-sequence of Horse Spleen Apoferritin FEBS Letters. ,vol. 129, pp. 322- 327 ,(1981) , 10.1016/0014-5793(81)80193-7
Erika R. Bauminger, Pauline M. Harrison, Daniel Hechel, Israel Nowik, Amyra Treffry, Mössbauer spectroscopic investigation of structure-function relations in ferritins. Biochimica et Biophysica Acta. ,vol. 1118, pp. 48- 58 ,(1991) , 10.1016/0167-4838(91)90440-B
Hsin-Sheng YANG, Mark JOHNSON, Mulchand S. PATEL, Roles of an Ets motif and a novel CACGAC direct repeat in transcription of the murine dihydrolipoamide dehydrogenase (Dld) gene. Biochemical Journal. ,vol. 338, pp. 667- 675 ,(1999) , 10.1042/BJ3380667