Heme-copper assembly mediated reductive coupling of nitrogen monoxide (*NO).

N(2)O + ligand-Cu(II)(NO(2)(-)). The chemical system described represents a (stoichiometric) functional model for heme/Cu protein nitric oxide reductase activity. -->
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Grant Information: R01 GM060353 United States GM NIGMS NIH HHS; R01 GM060353-08S1 United States GM NIGMS NIH HHS; GM 60353 United States GM NIGMS NIH HHS
Substance Nomenclature: 0 (Ferric Compounds)
0 (Nitrites)
14448-38-5 (hyponitrite)
31C4KY9ESH (Nitric Oxide)
42VZT0U6YR (Heme)
789U1901C5 (Copper)
S7G510RUBH (Nitrogen Dioxide)
Entry Date(s): Date Created: 20081223 Date Completed: 20090325 Latest Revision: 20211020
Update Code: 20221213
PubMed Central ID: PMC2662328
DOI: 10.1021/ja8084324
PMID: 19099478
Autor: Wang J; Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, USA., Schopfer MP, Sarjeant AA, Karlin KD
Jazyk: angličtina
Zdroj: Journal of the American Chemical Society [J Am Chem Soc] 2009 Jan 21; Vol. 131 (2), pp. 450-1.
DOI: 10.1021/ja8084324
Abstrakt: A iron-dinitrosyl species ((6)L)Fe(NO)(2) (2), generated from nitrogen monoxide (*NO) binding to its related iron(II)-mononitrosyl complex ((6)L)Fe(NO) (1), efficiently effects reductive coupling of two *NO molecules to release nitrous oxide (N(2)O), when Cu(+) ion and 2 equiv acid are added; the heme/Cu product is [((6)L)Fe(III)...Cu(II)(D)](3+) (D = H(2)O or MeCN). In a control experiment where only ((6)L)Fe(NO)(2) (2) is exposed to 2 equiv acid, no UV-vis change is observed; upon warming, *NO((g)) is released and ((6)L)Fe(NO) is reformed. The copper ion complex within the (6)L ligand framework is required for the *NO coupling chemistry. In a further control experiment Cu(+) ion is added to ((6)L)Fe(NO)(2) without acid present, [((6)L)Fe(NO)...Cu(II)(NO(2)(-))](+) is obtained, with the amount of N(2)O((g)) released fitting with copper(I) ion promoted disproportionation chemistry, 3*NO + ligand-Cu(I) --> N(2)O + ligand-Cu(II)(NO(2)(-)). The chemical system described represents a (stoichiometric) functional model for heme/Cu protein nitric oxide reductase activity.
Databáze: MEDLINE