Product formation and kinetic simulations in the pH range 1–14 account for a free-radical mechanism of peroxynitrite decomposition

Kirsch, Michael; Korth, Hans Gert; Wensing, Angela; Sustmann, Reiner; Groot, Herbert de

doi:10.1016/j.abb.2003.07.002

Cited by 69 publications

(91 citation statements)

References 112 publications

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“…Evidence for production of a nitrosyl complex was not reported in the original stopped-flow kinetic results from reactions of CYP102 with PN (14), which resembled the results found here for reaction of CYP119 with PN, and kinetics were not followed in the more recent study (16). It seems possible that the CYP102 nitrosyl complex might be formed after PN decays because a major decomposition product from PN at neutral pH is nitrite (26,27), and nitrite is known to react with various iron-containing enzymes (29). In studies of nitrite reactions with P450 cam and CPO, the formation of nitrosyl complexes was inferred from UV-visible spectra (29-31).…”

Section: Resultsmentioning

confidence: 61%

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X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Newcomb

Halgrimson

Horner

et al. 2008

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

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The cytochrome P450 enzyme CYP119, its compound II derivative, and its nitrosyl complex were studied by iron K-edge x-ray absorption spectroscopy. The compound II derivative was prepared by reaction of the resting enzyme with peroxynitrite and had a lifetime of Ϸ10 s at 23°C. The CYP119 nitrosyl complex was prepared by reaction of the enzyme with nitrogen monoxide gas or with a nitrosyl donor and was stable at 23°C for hours. Samples of CYP119 and its derivatives were studied by x-ray absorption spectroscopy at temperatures below 140 (K) at the Advanced Photon Source of Argonne National Laboratory. The x-ray absorption near-edge structure spectra displayed shifts in edge and pre-edge energies consistent with increasing effective positive charge on iron in the series native CYP119 < CYP119 nitrosyl complex < CYP119 compound II derivative. Extended x-ray absorption fine structure spectra were simulated with good fits for k ‫؍‬ 12 Å ؊1 for native CYP119 and k ‫؍‬ 13 Å ؊1 for both the nitrosyl complex and the compound II derivative. The important structural features for the compound II derivative were an iron-oxygen bond length of 1.82 Å and an iron-sulfur bond length of 2.24 Å, both of which indicate an iron-oxygen single bond in a ferryl-hydroxide, Fe IV OH, moiety.EXAFS ͉ ferryl-oxo ͉ XANES

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Section: Resultsmentioning

confidence: 61%

“…PN is prepared and stored in basic solutions (24). It is highly reactive with many biological substrates (25), and it rapidly decays in neutral solutions through an acid-catalyzed process giving approximately equal amounts of nitrate and nitrite (26)(27)(28). In addition, iron-containing enzymes catalyze the decomposition of PN (13,25).…”

Section: Resultsmentioning

confidence: 99%

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Newcomb

Halgrimson

Horner

et al. 2008

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

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“…Kinetic Simulations-The kinetic simulation was carried out using a freely available software, Kintecus 4.55 (61). The kinetic model used in this study is a modification of the published model (62). The list of the chemical reactions, rate constants, and major modifications used in the simulation is shown in supplemental Table S1.…”

Section: Methodsmentioning

confidence: 99%

Nitroxyl (HNO) Reacts with Molecular Oxygen and Forms Peroxynitrite at Physiological pH

Smulik

Dębski

Zielonka

et al. 2014

Journal of Biological Chemistry

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Background: Nitroxyl (HNO) is a reactive nitrogen species implicated in cardioprotection. Results: Nitroxyl reacts with oxygen to form an oxidizing and nitrating species, peroxynitrite. Conclusion: In the presence of oxygen, HNO donors may be a source of peroxynitrite. Significance: Peroxynitrite formation should be taken into account in the extracellular milieu when exposing cells to HNO donor under aerobic conditions.

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“…The kinetic model used in this study is a modification of the published model of peroxynitrite decay (37). The list of the chemical reactions, rate constants, and major modifications used in the simulation is shown in supplemental Table S1.…”

Section: Quantitation Of Onoomentioning

confidence: 99%

Peroxynitrite Is the Major Species Formed from Different Flux Ratios of Co-generated Nitric Oxide and Superoxide

Zielonka

Sikora

Joseph

et al. 2010

Journal of Biological Chemistry

200

180

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There is much interest in the nitration. , Reaction 1,The early indication of the occurrence of this reaction in biological systems came from the report on the inhibitory effect of O 2 . on the activity of endothelium-derived relaxing factor (7).After endothelium-derived relaxing factor identity was established as ⅐ NO (8, 9), its scavenging by O 2 . was first proposed as a contributing factor to endothelial injury (10). Reaction 1 has great physiological significance as both ⅐ NO and hydrogen peroxide (H 2 O 2 , the product of dismutation of O 2 . ) act as important second messengers in redox cell signaling (11,12). In the absence of scavengers, ONOO Ϫ decomposes at neutral pH via protonation to peroxynitrous acid (pK a ϭ 6.7, Reaction 2) to yield nitrate (NO 3 Ϫ ) and free radical intermediates:hydroxyl radical ( ⅐ OH) and nitrogen dioxide ( ⅐ NO 2 ) (Reaction 3, k 3 ϭ 1.25 s Ϫ1 ) (2, 13).In most biological systems, carbon dioxide is a likely scavenger of ONOO Ϫ , yielding a short-lived nitrosoperoxycarbonate anion (ONOOCO 2 Ϫ , Reaction 4, k 4 ϭ 2.9 ϫ 10 4 M Ϫ1 s Ϫ1 (14)). During the decomposition of ONOOCO 2 Ϫ , nitrate and carbon dioxide are formed, as well as nitrogen dioxide radical and carbonate radical anion (Reaction 5) (2, 13, 15).Due to the occurrence of Reactions 4 and 5, as well as the scavenging by peroxiredoxins or oxyhemoglobin in specific subcellular compartments, the lifetime of ONOO Ϫ in biological systems is limited to only a few milliseconds (2, 13). The current methodologies for detection of ONOO Ϫ are based on the detection of radical species formed from ONOO Ϫ decomposition, i.e. ⅐ NO 2 and CO 3 . or ⅐ OH, using tyrosine that forms nitrotyrosine (TyrNO 2 ) as a marker product of intracellular ⅐ NO 2 and dihydrorhodamine 123 (DHR) 2 as a fluorogenic probe for oxidants ( ⅐ NO 2 , ⅐ OH, CO 3 . ). However, ⅐ NO 2 radical formed from the ONOO Ϫ -independent processes, e.g. via myeloperoxidasecatalyzed oxidation of nitrite by H 2 O 2 (16), could make data interpretation more tenuous (17, 18). Additional problems with this indirect approach may arise from alternate mechanisms through which TyrNO 2 can be formed without the involvement of ⅐ NO 2 radicals (19). DHR can be oxidized to the fluorescent rhodamine molecule by various one-electron oxidants, including compounds I and II of peroxidases (20,21 2 The abbreviations used are: DHR, dihydrorhodamine 123; CBA, coumarin-7-boronic acid; CBE, coumarin-7-boronic acid, pinacolate ester; COH, 7-hydroxycoumarin; PAPA-NONOate, (Z)-1-[N-(3-ammoniopropyl)-N-(n-propyl)amino]diazen-1-ium-1,2-diolate; X, xanthine; XO, xanthine oxidase; SOD, superoxide dismutase; DTPA, diethylenetriaminepentaacetic acid; HPLC, high pressure liquid chromatography.

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Product formation and kinetic simulations in the pH range 1–14 account for a free-radical mechanism of peroxynitrite decomposition

Cited by 69 publications

References 112 publications

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Nitroxyl (HNO) Reacts with Molecular Oxygen and Forms Peroxynitrite at Physiological pH

Peroxynitrite Is the Major Species Formed from Different Flux Ratios of Co-generated Nitric Oxide and Superoxide

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