NDLI: Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.

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Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Landry, Aaron P. Duan, Xuewu Huang, Hao Ding, Huangen
Description	Country affiliation: United States Author Affiliation: Landry AP ( Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA.)
Abstract	Protein-bound dinitrosyl iron complexes (DNICs) have been observed in prokaryotic and eukaryotic cells under nitric oxide (NO) stress. The identity of proteins that bind DNICs, however, still remains elusive. Here we demonstrate that iron-sulfur proteins are the major source of protein-bound DNICs formed in Escherichia coli cells under NO stress. Expression of recombinant iron-sulfur proteins, but not proteins without iron-sulfur clusters, almost doubles the amount of protein-bound DNICs formed in E. coli cells after NO exposure. Purification of recombinant proteins from the NO-exposed E. coli cells further confirms that iron-sulfur proteins, but not proteins without iron-sulfur clusters, are modified, forming protein-bound DNICs. Deletion of the iron-sulfur cluster assembly proteins IscA and SufA to block the [4Fe-4S] cluster biogenesis in E. coli cells largely eliminates the NO-mediated formation of protein-bound DNICs, suggesting that iron-sulfur clusters are mainly responsible for the NO-mediated formation of protein-bound DNICs in cells. Furthermore, depletion of the 'chelatable iron pool' in wild-type E. coli cells effectively removes iron-sulfur clusters from proteins and concomitantly diminishes the NO-mediated formation of protein-bound DNICs, indicating that iron-sulfur clusters in proteins constitute at least part of the chelatable iron pool in cells.
File Format	HTM / HTML
ISSN	08915849
e-ISSN	18734596
DOI	10.1016/j.freeradbiomed.2011.03.005
Journal	Free Radical Biology and Medicine
Issue Number	11
Volume Number	50
Language	English
Publisher	Elsevier
Publisher Date	2011-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Free radicals biology Escherichia Coli Proteins Metabolism Escherichia Coli Physiology Iron Chelating Agents Iron-sulfur Proteins Nitrogen Oxides Cloning, Molecular Electron Spin Resonance Spectroscopy Chemistry Genetics Nitric Oxide Oxidative Stress Protein Binding Protein Processing, Post-translational Recombinant Proteins Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology (medical) Biochemistry

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Iron-sulfur Proteins Are the Major Source of Protein-bound Dinitrosyl Iron Complexes Formed in Escherichia coli Cells under Nitric Oxide Stress

Oxygen is required for the L-cysteine-mediated decomposition of protein-bound dinitrosyl-iron complexes.

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Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.

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Iron-sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress.