Formation of Peroxynitrite from Reaction of Nitroxyl Anion with Molecular Oxygen

Kirsch, Michael; Groot, Herbert de

doi:10.1074/jbc.m108079200

Cited by 98 publications

(94 citation statements)

References 72 publications

(79 reference statements)

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“…This tiny decrease is again explained by the GS Ϫ -dependent side reaction. Reaction of low molecular weight S-nitrosothiols with thiols has been reported to yield nitroxyl (18), which generates strong oxidants like peroxynitrite (19), and tryptophan is a very good target for this peroxide and the radicals derived from it (20 -22). Thus, the GSH-dependent denitrosation of NANT most likely yielded stoichiometric amounts of NAT, thereby fully restituting the indole ring during this transnitrosation reaction.…”

Section: Resultsmentioning

confidence: 99%

Formation of S-Nitrosothiols from Regiospecific Reaction of Thiols with N-Nitrosotryptophan Derivatives

Sonnenschein¹,

Groot

Kirsch

2004

Journal of Biological Chemistry

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Section: Resultsmentioning

confidence: 99%

Formation of S-Nitrosothiols from Regiospecific Reaction of Thiols with N-Nitrosotryptophan Derivatives

Sonnenschein¹,

Groot

Kirsch

2004

Journal of Biological Chemistry

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“…It is widely accepted that HNO and singlet oxygen can react to form PN [52]. Thus, the ability of AsPrx-4783 to protect against HNO may be due in part to PN reductase activity of AsPrx-4783.…”

Section: Discussionmentioning

confidence: 99%

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

Peterson

Luckhart

2006

Free Radical Biology and Medicine

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Malaria parasite infection in anopheline mosquitoes induces nitrosative and oxidative stresses that limit parasite development, but also damage mosquito tissues in proximity to the response. Based on these observations, we proposed that cellular defenses in the mosquito may be induced to minimize self-damage. Specifically, we hypothesized that peroxiredoxins (Prxs), enzymes known to detoxify reactive oxygen species (ROS) and reactive nitrogen oxide species (RNOS), protect mosquito cells. We identified an Anopheles stephensi 2-Cys Prx ortholog of Drosophila melanogaster Prx-4783, which protects fly cells against oxidative stresses. To assess function, AsPrx-4783 was overexpressed in D. melanogaster (S2) and in A. stephensi (MSQ43) cells and silenced in MSQ43 cells with RNA interference before treatment with various ROS and RNOS. Our data revealed that AsPrx-4783 and DmPrx-4783 differ in host cell protection and that AsPrx-4783 protects A. stephensi cells against stresses that are relevant to malaria parasite infection in vivo, namely nitric oxide (NO), hydrogen peroxide, nitroxyl, and peroxynitrite. Further, AsPrx-4783 expression is induced in the mosquito midgut by parasite infection at times associated with peak nitrosative and oxidative stresses. Hence, whereas the NO-mediated defense response is toxic to both host and parasite, AsPrx-4783 may shift the balance in favor of the mosquito. KeywordsMalaria; Mosquito; Peroxiredoxin; Plasmodium; Anopheles; Nitric oxide; Nitrosative stress; Free radicals It has long been recognized that reactive oxygen species (ROS) and, more recently, reactive nitrogen oxide species (RNOS) function to defend hosts against pathogens [1]. Although ROS and RNOS are cytotoxic to pathogens and parasites, they also induce oxidative and nitrosative stresses in the host and can damage host tissues [1]. Host protection against oxidative and nitrosative stress, therefore, is vital for homeostasis and hence survival. Gene products that confer protection against ROS are well known. In contrast, gene products that confer protection against RNOS have been identified, but are less well studied. The peroxiredoxins (Prxs) are a recently discovered family of antioxidant peroxidases that can reduce hydrogen peroxide and alkyl hydroperoxides to water and the corresponding alcohols, respectively, and can protect cells from widely divergent organisms against a variety of nitrosative stress challenges [2][3][4][5][6].Prxs do not show sequence homology to other known antioxidant enzymes. Crystal structures of PrxI, II, V, and VI have revealed that Prxs are novel members of the thioredoxin fold * Corresponding author. Fax: +1 530 752 8692. E-mail address: sluckhart@ucdavis.edu (S. Luckhart). NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript superfamily [7,8]. Unlike most peroxidases-which contain a heme ring at their active site (e.g., cytochrome c peroxidase) or a redox-sensitive moiety like selenocysteine (glutathione peroxidase; GPx), vanadium (algal bro...

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“…It should be remembered that harmful reactions are also known for S-nitrosothiols. For example, it has been reported that S-nitrosothiols react with thiols to yield nitroxyl (48), which generates hydroxyl radicals and/or peroxynitrite in the absence and presence of oxygen, respectively (49). Because N-nitrosotryptophan derivatives are rather longlived and yet not "indefinitely" stable compounds (the hydrolysis of N-acetyl-N-nitrosotryptophan is expected to yield the harmless products tryptophan and nitrite (28)), one may speculate that this could further decrease the putative mutagenic potential of N-nitrosotryptophan.…”

Section: Discussionmentioning

confidence: 99%

Regiospecific Nitrosation of N-terminal-blocked Tryptophan Derivatives by N2O3 at Physiological pH

Kirsch¹,

Fuchs²,

Groot

2003

Journal of Biological Chemistry

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Nitric oxide ( ⅐ NO) is involved in a great variety of physiological and pathophysiological processes, including the regulation of vascular tonus, immune response, and neurotransmission (1). In mammals the basal level of ⅐ NO (in the aqueous phase) is in the nanomolar range (2). However, the local ⅐ NO concentrations can be increased substantially in areas with high NO synthase activity and/or in hydrophobic regions (3, 4), thereby facilitating the formation of dinitrogen trioxide (N 2 O 3 ) (Equations 1 (5) and 2 (6)).2 ⅐ NO ϩ O 2 3 2 ⅐ NO 2 k 1 ϭ 2.9 ϫ 10 6 M Ϫ2 s Ϫ1

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Formation of Peroxynitrite from Reaction of Nitroxyl Anion with Molecular Oxygen

Abstract: Peroxynitrite (ONOOpathway.

Cited by 98 publications

References 72 publications

Formation of S-Nitrosothiols from Regiospecific Reaction of Thiols with N-Nitrosotryptophan Derivatives

Formation of S-Nitrosothiols from Regiospecific Reaction of Thiols with N-Nitrosotryptophan Derivatives

A mosquito 2-Cys peroxiredoxin protects against nitrosative and oxidative stresses associated with malaria parasite infection

Regiospecific Nitrosation of N-terminal-blocked Tryptophan Derivatives by N2O3 at Physiological pH

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