大肠杆菌细菌铁蛋白中非血红素铁位点的电子顺磁共振研究及其与磷酸盐的相互作用。一项使用一氧化氮作为自旋探针的研究。

An EPR investigation of non-haem iron sites in Escherichia coli bacterioferritin and their interaction with phosphate. A study using nitric oxide as a spin probe.

作者信息

Le Brun N E, Cheesman M R, Thomson A J, Moore G R, Andrews S C, Guest J R, Harrison P M

机构信息

Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, UK.

出版信息

FEBS Lett. 1993 Jun 1;323(3):261-6. doi: 10.1016/0014-5793(93)81353-2.

DOI:10.1016/0014-5793(93)81353-2

PMID:8388809

Abstract

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.

摘要

对大肠杆菌的铁储存蛋白细菌铁蛋白（BFR）的电子顺磁共振（EPR）研究【1993年，《生物化学杂志》第292卷，第47 - 56页】表明，在蛋白质外壳内存在非血红素铁（III）（NHI）位点，这些位点可能参与铁的摄取和释放。当一氧化氮用作NHI位点Fe（II）状态的EPR自旋探针时，发现了两种不同的单核NHI物种。在某些条件下，还观察到了铁二聚体。已经研究了磷酸盐与NHI物种的反应。结果表明该阴离子在核心成核中具有一定作用。