Nitroxyl (azanone) trapping by metalloporphyrins

Doctorovich, Fabio; Bikiel, Damián E.; Pellegrino, Juan; Suárez, Sebastián; Larsen, Anna; Marti, Marcelo Adrian

doi:10.1016/j.ccr.2011.04.012

Cited by 87 publications

(107 citation statements)

References 185 publications

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“…This includes the HNO-donor molecule cyanamide (N-hydroxycyanamide is the actual HNO-donor), which has shown to be an effective anti-alcoholism drug by disturbing alcohol metabolism through inhibiting the enzyme aldehyde dehydrogenase [7,8]. The mechanism of action of HNO appears to be through its interactions with thiol-containing biomolecules [9][10][11] and ferric heme proteins [1,[12][13][14][15][16]. While the endogenous production of HNO has not been clearly established, there is evidence of its formation from nitric oxide synthase (NOS) in the absence of its biopterin cofactor [17].…”

Section: Introductionmentioning

confidence: 99%

Synthesis, properties, and reactivity of a series of non-heme {FeNO}7/8 complexes: Implications for Fe-nitroxyl coordination

Sanders

Patra

Harrop

2013

Journal of Inorganic Biochemistry

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Section: Introductionmentioning

confidence: 99%

Synthesis, properties, and reactivity of a series of non-heme {FeNO}7/8 complexes: Implications for Fe-nitroxyl coordination

Sanders

Patra

Harrop

2013

Journal of Inorganic Biochemistry

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“…But the observed regioselectivity of the nitroxygenase reactivity demands that an N radical, the alpha-atom attached to the metal in B 0 , couples to the substrate radical. The HNO adduct is depicted as N bound, as found in characterized end-on HNO-metal complexes (58). There is much recent evidence for O-bound linkage isomers of metal-nitrosyls, termed isonitrosyls, but these are typically only observed after photolysis at low temperature within a solid or crystalline material (59)(60)(61)(62).…”

Section: Discussionmentioning

confidence: 99%

Nitrosyl hydride (HNO) replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase

Kumar

Zapata

Ramirez

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Quercetin dioxygenase (QDO) catalyzes the oxidation of the flavonol quercetin with dioxygen, cleaving the central heterocyclic ring and releasing CO. The QDO from Bacillus subtilis is unusual in that it has been shown to be active with several divalent metal cofactors such as Fe, Mn, and Co. Previous comparison of the catalytic activities suggest that Mn(II) is the preferred cofactor for this enzyme. We herein report the unprecedented substitution of nitrosyl hydride (HNO) for dioxygen in the activity of Mn-QDO, resulting in the incorporation of both N and O atoms into the product. Turnover is demonstrated by consumption of quercetin and other related substrates under anaerobic conditions in the presence of HNO-releasing compounds and the enzyme. As with dioxygenase activity, a nonenzymatic base-catalyzed reaction of quercetin with HNO is observed above pH 7, but no enhancement of this basal reactivity is found upon addition of divalent metal salts. Unique and regioselective N-containing products ( 14 N∕ 15 N) have been characterized by MS analysis for both the enzymatic and nonenzymatic reactions. Of the several metallo-QDO enzymes examined for nitroxygenase activity under anaerobic condition, only the Mn(II) is active; the Fe(II) and Co(II) substituted enzymes show little or no activity. This result represents an enzymatic catalysis which we denote nitroxygenase activity; the unique reactivity of the Mn-QDO suggests a metalmediated electron transfer mechanism rather than metal activation of the substrate's inherent base-catalyzed reactivity.nitroxyl | quercetinase D ioxygenases are enzymes that incorporate both atoms of dioxygen into a targeted substrate, e.g., the enzyme catechol 1,2-dioxygenase cleaves the C-C bond between catechol's two hydroxyl groups forming the dicarboxylate cis,cis-muconic acid (1). Although highly divergent, there are two broadly defined classes of nonheme dioxygenases: those that directly bind dioxygen at the metal center or those in which dioxygen binds to the substrate that has been activated by interaction with the metal center (2). Such questions also apply to quercetin dioxygenase (QDO), which catalyzes the oxidation of the flavonol quercetin (1) with dioxygen ( Fig. 1). During turnover, QDO cleaves the central heterocyclic ring of quercetin, releasing CO, and yielding the corresponding depside. The QDO from Bacillus subtilis is unusual in that it has been shown to be active with several divalent metal cofactors such as Cu, Fe, Mn, and Co. Comparison of the catalytic activities suggest that Mn(II) is the preferred cofactor for this enzyme (3).The simple molecule nitrosyl hydride (HNO) is the singly reduced and protonated form of nitric oxide, NO. HNO has garnered much interest because it demonstrates a physiological reactivity distinctly different from its congener nitric oxide (4, 5). In a series of papers, we have reported the preparation and characterization of the HNO adduct of myoglobin (HNO-Mb) by reduction of 7) and by trapping of free HNO by deoxymyoglobin (Mb-Fe II ) (8)...

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“…The chemistry of HNO and the formation and reactions of HNO metal complexes have been extensively reviewed [158][159][160][161].…”

Section: Protonation Of Metal Nitrosylsmentioning

confidence: 99%

Mechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers

Ford

Pereira

Miranda

2013

Nitrosyl Complexes in Inorganic Chemistry, Biochemistry and Medicine II

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Nitroxyl (azanone) trapping by metalloporphyrins

Cited by 87 publications

References 185 publications

Synthesis, properties, and reactivity of a series of non-heme {FeNO}7/8 complexes: Implications for Fe-nitroxyl coordination

Synthesis, properties, and reactivity of a series of non-heme {FeNO}7/8 complexes: Implications for Fe-nitroxyl coordination

Nitrosyl hydride (HNO) replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenase

Mechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers

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