| pubmed-article:18945212 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18945212 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:18945212 | lifeskim:mentions | umls-concept:C0028128 | lld:lifeskim |
| pubmed-article:18945212 | lifeskim:mentions | umls-concept:C1704332 | lld:lifeskim |
| pubmed-article:18945212 | lifeskim:mentions | umls-concept:C0058132 | lld:lifeskim |
| pubmed-article:18945212 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:18945212 | pubmed:dateCreated | 2009-1-12 | lld:pubmed |
| pubmed-article:18945212 | pubmed:abstractText | Although the NO (nitric oxide)-mediated modification of iron-sulfur proteins has been well-documented in bacteria and mammalian cells, specific reactivity of NO with iron-sulfur proteins still remains elusive. In the present study, we report the first kinetic characterization of the reaction between NO and iron-sulfur clusters in protein using the Escherichia coli IlvD (dihydroxyacid dehydratase) [4Fe-4S] cluster as an example. Combining a sensitive NO electrode with EPR (electron paramagnetic resonance) spectroscopy and an enzyme activity assay, we demonstrate that NO is rapidly consumed by the IlvD [4Fe-4S] cluster with the concomitant formation of the IlvD-bound DNIC (dinitrosyl-iron complex) and inactivation of the enzyme activity under anaerobic conditions. The rate constant for the initial reaction between NO and the IlvD [4Fe-4S] cluster is estimated to be (7.0+/-2.0)x10(6) M(-2) x s(-1) at 25 degrees C, which is approx. 2-3 times faster than that of the NO autoxidation by O2 in aqueous solution. Addition of GSH failed to prevent the NO-mediated modification of the IlvD [4Fe-4S] cluster regardless of the presence of O2 in the medium, further suggesting that NO is more reactive with the IlvD [4Fe-4S] cluster than with GSH or O2. Purified aconitase B [4Fe-4S] cluster from E. coli has an almost identical NO reactivity as the IlvD [4Fe-4S] cluster. However, the reaction between NO and the endonuclease III [4Fe-4S] cluster is relatively slow, apparently because the [4Fe-4S] cluster in endonuclease III is less accessible to solvent than those in IlvD and aconitase B. When E. coli cells containing recombinant IlvD, aconitase B or endonuclease III are exposed to NO using the Silastic tubing NO delivery system under aerobic and anaerobic conditions, the [4Fe-4S] clusters in IlvD and aconitase B, but not in endonuclease III, are efficiently modified forming the protein-bound DNICs, confirming that NO has a higher reactivity with the [4Fe-4S] clusters in IlvD and aconitase B than with O2 or GSH. The results suggest that the iron-sulfur clusters in proteins such as IlvD and aconitase B may constitute the primary targets of the NO cytotoxicity under both aerobic and anaerobic conditions. | lld:pubmed |
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| pubmed-article:18945212 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18945212 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18945212 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18945212 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18945212 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:18945212 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:18945212 | pubmed:author | pubmed-author:DingHuangenH | lld:pubmed |
| pubmed-article:18945212 | pubmed:author | pubmed-author:RenBinbinB | lld:pubmed |
| pubmed-article:18945212 | pubmed:author | pubmed-author:YangJuanjuanJ | lld:pubmed |
| pubmed-article:18945212 | pubmed:author | pubmed-author:DuanXuewuX | lld:pubmed |
| pubmed-article:18945212 | pubmed:author | pubmed-author:TanGuoqiangG | lld:pubmed |
| pubmed-article:18945212 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18945212 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:18945212 | pubmed:volume | 417 | lld:pubmed |
| pubmed-article:18945212 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18945212 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18945212 | pubmed:pagination | 783-9 | lld:pubmed |
| pubmed-article:18945212 | pubmed:dateRevised | 2010-12-28 | lld:pubmed |
| pubmed-article:18945212 | pubmed:meshHeading | pubmed-meshheading:18945212... | lld:pubmed |
| pubmed-article:18945212 | pubmed:meshHeading | pubmed-meshheading:18945212... | lld:pubmed |
| pubmed-article:18945212 | pubmed:meshHeading | pubmed-meshheading:18945212... | lld:pubmed |
| pubmed-article:18945212 | pubmed:meshHeading | pubmed-meshheading:18945212... | lld:pubmed |
| pubmed-article:18945212 | pubmed:meshHeading | pubmed-meshheading:18945212... | lld:pubmed |
| pubmed-article:18945212 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:18945212 | pubmed:articleTitle | Reactivity of nitric oxide with the [4Fe-4S] cluster of dihydroxyacid dehydratase from Escherichia coli. | lld:pubmed |
| pubmed-article:18945212 | pubmed:affiliation | Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA. | lld:pubmed |
| pubmed-article:18945212 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18945212 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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