AN EPR INVESTIGATION OF NONHEME IRON SITES IN ESCHERICHIA-COLI BACTERIOFERRITIN AND THEIR INTERACTION WITH PHOSPHATE - A STUDY USING NITRIC-OXIDE AS A SPIN PROBE

被引：25

作者：

LEBRUN, NF

CHEESMAN, MR

THOMSON, AJ

MOORE, GR

ANDREWS, SC

GUEST, JR

HARRISON, PM

机构：

[1] UNIV E ANGLIA,SCH CHEM SCI,CTR MET PROT SPECT & BIOL,NORWICH NR4 7TJ,NORFOLK,ENGLAND

[2] UNIV SHEFFIELD,KREBS INST,DEPT MOLEC BIOL & BIOTECHNOL,SHEFFIELD S10 2TN,S YORKSHIRE,ENGLAND

来源：

FEBS LETTERS | 1993年 / 323卷 / 03期

基金：

英国惠康基金;

关键词：

BACTERIOFERRITIN (BFR); NHI SITE; NITRIC OXIDE; PHOSPHATE;

D O I：

10.1016/0014-5793(93)81353-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

EPR studies of bacterioferritin (BFR), an iron-storage protein of Escherichia coli [1993, Biochem. J. 292, 47-56.], have revealed the presence of non-haem iron (III) (NHI) sites within the protein coat which may be involved in iron uptake and release. When nitric oxide was used as an EPR spin probe of the Fe(II) state of the NHI sites, two distinct mononuclear NHI species were found. Under certain conditions, an iron dimer was also observed. The reaction of phosphate with NHI species has been investigated. Results point to a function for this anion in core nucleation.

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收藏

页码：261 / 266

页数：6

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