Chemistry of Peroxynitrites as Compared to Peroxynitrates

Goldstein, Sara; Lind, Johan; Merényi, Gábor

doi:10.1021/cr0307087

Cited by 367 publications

(364 citation statements)

References 179 publications

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344

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“…Ml-trHbOAFe(IV)@O in the absence of CO 2 (=6.7 ± 0.1) corresponds to that reported for the ONOOH M ONOO À equilibrium (=6.5-6.8) (see [14]). Therefore, k lim(top) should represent k on for Ml-trHbOAFe(IV)@O reduction to Ml-trHbOAFe(III) by ONOOH at pH ( pK a , while k lim(bottom) should be referred to k on for Ml-trHbOAFe(IV)@O reduction to Ml-trHbOAFe(III) by ONOO À at pH ) pK a .…”

Section: Ml-trhbo-fe(iv)=o + Peroxynitritesupporting

confidence: 80%

“…The peroxynitrite concentration was determined spectrophotometrically at 302 nm (e 302 nm = 1.705 Â 10 3 M À1 cm À1 ) [35,36]. Decomposed peroxynitrite was obtained by acidification of the peroxynitrite solution [14].…”

Section: Methodsmentioning

confidence: 99%

“…) and Å NO 2 [11][12][13][14][15][16]. Note that leukocyte peroxidase catalyzes peroxynitrite conversion to hydrogen-peroxide-halide, representing an efficient antimicrobial agent.…”

Section: åàmentioning

confidence: 99%

“…1 The recommended IUPAC nomenclature for peroxynitrite is oxoperoxonitrate (1 À ) and for peroxynitrous acid is hydrogen oxoperoxonitrate. The term peroxynitrite is used in the text to refer generically to both ONOO À and its conjugate acid ONOOH (see [14]). [25,26,[30][31][32]).…”

Section: åàmentioning

confidence: 99%

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Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O

Ascenzi¹,

Marinis²,

Visca³

et al. 2009

Biochemical and Biophysical Research Communications

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Section: Ml-trhbo-fe(iv)=o + Peroxynitritesupporting

confidence: 80%

Section: Methodsmentioning

confidence: 99%

“…) and Å NO 2 [11][12][13][14][15][16]. Note that leukocyte peroxidase catalyzes peroxynitrite conversion to hydrogen-peroxide-halide, representing an efficient antimicrobial agent.…”

Section: åàmentioning

confidence: 99%

Section: åàmentioning

confidence: 99%

See 2 more Smart Citations

Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O

Ascenzi¹,

Marinis²,

Visca³

et al. 2009

Biochemical and Biophysical Research Communications

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“…Peroxynitrite-NO undergoes a variety of oxidative and radical reactions generating a number of stable reaction products and intermediates with a wide range of stability and reactivity [125]. One such a product, the peroxynitrite anion (ONOO − ), has attracted wide attention in the area of NO research.…”

Section: 2mentioning

confidence: 99%

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

Boudko

2007

Journal of Chromatography B

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This review briefly summarizes recent progress in fundamental understanding and analytical profiling of the L-arginine/nitric oxide (NO) pathway. It focuses on key analytical references of NO actions and on the experimental acquisition of these references in vivo, with capillary electrophoresis (CE) and high-performance capillary electrophoresis (HPCE) comprising one of the most flexible and technologically promising analytical platform for comprehensive high-resolution profiling of NO-related metabolites. Second aim of this review is to express demands and bridge efforts of experimental biologists, medical professionals and chemical analysis-oriented scientists who strive to understand evolution and physiological roles of NO and to develop analytical methods for use in biology and medicine.

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Human nitrobindin: the first example of an all‐β‐barrel ferric heme‐protein that catalyzes peroxynitrite detoxification

Masi

Polticelli

et al. 2018

FEBS Open Bio

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Nitrobindins (Nbs), constituting a heme‐protein family spanning from bacteria to Homo sapiens , display an all‐β‐barrel structural organization. Human Nb has been described as a domain of the nuclear protein named THAP 4, whose physiological function is still unknown. We report the first evidence of the heme‐Fe( III )‐based detoxification of peroxynitrite by the all‐β‐barrel C ‐terminal Nb‐like domain of THAP 4. Ferric human Nb (Nb( III )) catalyzes the conversion of peroxynitrite to and impairs the nitration of free l ‐tyrosine. The rate of human Nb( III )‐mediated scavenging of peroxynitrite is similar to those of all‐α‐helical horse heart and sperm whale myoglobin and human hemoglobin, generally taken as the prototypes of all‐α‐helical heme‐proteins. The heme‐Fe( III ) reactivity of all‐β‐barrel human Nb( III ) and all‐α‐helical prototypical heme‐proteins possibly reflects the out‐to‐in‐plane transition of the heme‐Fe( III )‐atom preceding peroxynitrite binding. Human Nb( III ) not only catalyzes the detoxification of peroxynitrite but also binds NO , possibly representing a target of reactive nitrogen species.

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Chemistry of Peroxynitrites as Compared to Peroxynitrates

Cited by 367 publications

References 179 publications

Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O

Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O

Bioanalytical profile of the l-arginine/nitric oxide pathway and its evaluation by capillary electrophoresis

Human nitrobindin: the first example of an all‐β‐barrel ferric heme‐protein that catalyzes peroxynitrite detoxification

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