Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
2008-11-14
pubmed:abstractText
The interaction of nitric oxide (NO) with iron-sulfur cluster proteins results in degradation and breakdown of the cluster to generate dinitrosyl iron complexes (DNICs). In some cases the formation of DNICs from such cluster systems can lead to activation of a regulatory pathway or the loss of enzyme activity. In order to understand the basic chemistry underlying these processes, we have investigated the reactions of NO with synthetic [2Fe-2S] and [4Fe-4S] clusters. Reaction of excess NO(g) with solutions of [Fe2S2(SR)4](2-) (R = Ph, p-tolyl (4-MeC6H4), or 1/2 (CH2)2-o-C6H4) cleanly affords the respective DNIC, [Fe(NO)2(SR)2](-), with concomitant reductive elimination of the bridging sulfide ligands as elemental sulfur. The structure of (Et4N)[Fe(NO)2(S-p-tolyl)2] was verified by X-ray crystallography. Reactions of the [4Fe-4S] clusters, [Fe4S4(SR)4](2-) (R = Ph, CH2Ph, (t)Bu, or 1/2 (CH2)-m-C6H4) proceed in the absence of added thiolate to yield Roussin's black salt, [Fe4S3(NO)7](-). In contrast, (Et4N)2[Fe4S4(SPh)4] reacts with NO(g) in the presence of 4 equiv of (Et4N)(SPh) to yield the expected DNIC. For all reactions, we could reproduce the chemistry effected by NO(g) with the use of trityl-S-nitrosothiol (Ph3CSNO) as the nitric oxide source. These results demonstrate possible pathways for the reaction of iron-sulfur clusters with nitric oxide in biological systems and highlight the importance of thiolate-to-iron ratios in stabilizing DNICs.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
130
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15602-10
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Reactions of synthetic [2Fe-2S] and [4Fe-4S] clusters with nitric oxide and nitrosothiols.
pubmed:affiliation
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural