Redox conversions of dinitrosyl iron complexes with natural thiol-containing ligands

Borodulin, R. R.; Kubrina, L. N.; Сереженков, В. А.; Burbaev, D. Sh.; Mikoyan, V. D.; Vanin, Anatoly F.

doi:10.1016/j.niox.2013.07.004

Cited by 17 publications

(9 citation statements)

References 22 publications

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“…s −1 ) (Figure 4b). Indeed, the value of this second-order rate constant is close to that determined for Prx1Cys 52 nitrosation by GSNO (k Cys52 +NO = 15.4 ± 0.4 M −1 . s −1 ), following the trend of transnitrosation reactions having equilibrium constant values approaching 1.0 [6].…”

Section: Discussionsupporting

confidence: 80%

“…Therefore, most of the Prx1 oxidation in the presence of GSNO occurred before S-nitrosation ( Figure S1). The data presented up to this point supported S-nitrosation of two Cys residues in Prx1 by GSNO and allowed assignment of the faster reaction to Prx1-Cys 52 NO formation. The identity of the second residue undergoing S-nitrosation remained unaddressed here although a previous mass spectrometric study of CysNO-treated Prx1 indicated Cys 83 as the secondary nitrosation target [23].…”

Section: Kinetics and Products Of The Reaction Of Prx1 With Gsnosupporting

confidence: 54%

“…In solution, DNIC-GS exists in equilibrium between the binuclear (B-DNIC) and the mononuclear (M-DNIC) forms (reaction 1) [42,50,51]. Here, we used solutions at pH 7.4 containing about 93-95% B-DNIC form (diamagnetic, EPR silent) and 5-7% M-DNIC form (paramagnetic, EPR active) [42,52] that are referred to as DNIC-GS for simplicity. The concentration of these mixtures is reported in terms of the iron center.…”

Section: Interaction Of Prx1 With Dnic-gsmentioning

confidence: 99%

“…We did not determine which Prx1 His residue coordinates to DNIC because a comparison of the relative binding affinity of Prx1 Cys 52 and Prx1 His to the complex indicated that Prx1 Cys 52 is the preferential DNIC ligand. Indeed, time-dependent incubation of Prx1 with DNIC-GS with freezing of the samples to stop the processes showed that after 2 min, the EPR signal is essentially of axial symmetry but it is of rhombic symmetry after 30 min incubation (Figure 5c).…”

Section: Prx1 Residues Involved In the Coordination To Dnic-gsmentioning

confidence: 99%

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The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione

et al. 2020

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Protein S-nitrosation is an important consequence of NO●·metabolism with implications in physiology and pathology. The mechanisms responsible for S-nitrosation in vivo remain debatable and kinetic data on protein S-nitrosation by different agents are limited. 2-Cys peroxiredoxins, in particular Prx1 and Prx2, were detected as being S-nitrosated in multiple mammalian cells under a variety of conditions. Here, we investigated the kinetics of Prx1 S-nitrosation by nitrosoglutathione (GSNO), a recognized biological nitrosating agent, and by the dinitrosyl-iron complex of glutathione (DNIC-GS; [Fe(NO)2(GS)2]−), a hypothetical nitrosating agent. Kinetics studies following the intrinsic fluorescence of Prx1 and its mutants (C83SC173S and C52S) were complemented by product analysis; all experiments were performed at pH 7.4 and 25 ℃. The results show GSNO-mediated nitrosation of Prx1 peroxidatic residue ( k + N O C y s 52 = 15.4 ± 0.4 M−1. s−1) and of Prx1 Cys83 residue ( k + N O C y s 83 = 1.7 ± 0.4 M−1. s−1). The reaction of nitrosated Prx1 with GSH was also monitored and provided a second-order rate constant for Prx1Cys52NO denitrosation of k − N O C y s 52 = 14.4 ± 0.3 M−1. s−1. In contrast, the reaction of DNIC-GS with Prx1 did not nitrosate the enzyme but formed DNIC-Prx1 complexes. The peroxidatic Prx1 Cys was identified as the residue that more rapidly replaces the GS ligand from DNIC-GS ( k D N I C C y s 52 = 7.0 ± 0.4 M−1. s−1) to produce DNIC-Prx1 ([Fe(NO)2(GS)(Cys52-Prx1)]−). Altogether, the data showed that in addition to S-nitrosation, the Prx1 peroxidatic residue can replace the GS ligand from DNIC-GS, forming stable DNIC-Prx1, and both modifications disrupt important redox switches.

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Section: Discussionsupporting

confidence: 80%

Section: Kinetics and Products Of The Reaction Of Prx1 With Gsnosupporting

confidence: 54%

Section: Interaction Of Prx1 With Dnic-gsmentioning

confidence: 99%

Section: Prx1 Residues Involved In the Coordination To Dnic-gsmentioning

confidence: 99%

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The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione

et al. 2020

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“…As another experimental fact proving that the concept of d 7 electron configuration of iron in DNICs with thiol-containing ligands is true, we can mention the results of our studies related to reduction of these complexes [ 99 , 100 ]. We found out that reducing both M-DNICs and B-DNICs with glutathione based on the two-electron mechanism to the paramagnetic state with S = 1/2 and d 9 electron configuration of iron is possible, which is entirely consistent with the idea.…”

Section: {Fe(no) 2 } 7 Representation Of the Iron-dinitrosyl Unit (Or Formally D 7 mentioning

confidence: 88%

Physico-Chemistry of Dinitrosyl Iron Complexes as a Determinant of Their Biological Activity

Vanin

2021

IJMS

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In this article we minutely discuss the so-called “oxidative” mechanism of mononuclear form of dinitrosyl iron complexes (M-DNICs) formations proposed by the author. M-DNICs are proposed to be formed from their building material—neutral NO molecules, Fe2+ ions and anionic non-thiol (L−) and thiol (RS−) ligands based on the disproportionation reaction of NO molecules binding with divalent ion irons in pairs. Then a protonated form of nitroxyl anion (NO−) appearing in the reaction is released from this group and a neutral NO molecule is included instead. As a result, M-DNICs are produced. Their resonance structure is described as [(L−)2Fe2+(NO)(NO+)], in which nitrosyl ligands are represented by NO molecules and nitrosonium cations in equal proportions. Binding of hydroxyl ions with the latter causes conversion of these cations into nitrite anions at neutral pH values and therefore transformation of DNICs into the corresponding high-spin mononitrosyl iron complexes (MNICs) with the resonance structure described as [(L−)2Fe2+(NO)]. In case of replacing L− by thiol-containing ligands, which are characterized by high π-donor activity, electron density transferred from sulfur atoms to iron-dinitrosyl groups neutralizes the positive charge on nitrosonium cations, which prevents their hydrolysis, ensuring relatively a high stability of the corresponding M-DNICs with the resonance structure [(RS−)2Fe2+ (NO, NO+)]. Therefore, M-DNICs with thiol-containing ligands, as well as their binuclear analogs (B-DNICs, respective resonance structure [(RS−)2Fe2+2 (NO, NO+)2]), can serve donors of both NO and NO+. Experiments with solutions of B-DNICs with glutathione or N-acetyl-L-cysteine (B-DNIC-GSH or B-DNIC-NAC) showed that these complexes release both NO and NO+ in case of decomposition in the presence of acid or after oxidation of thiol-containing ligands in them. The level of released NO was measured via optical absorption intensity of NO in the gaseous phase, while the number of released nitrosonium cations was determined based on their inclusion in S-nitrosothiols or their conversion into nitrite anions. Biomedical research showed the ability of DNICs with thiol-containing ligands to be donors of NO and NO+ and produce various biological effects on living organisms. At the same time, NO molecules released from DNICs usually have a positive and regulatory effect on organisms, while nitrosonium cations have a negative and cytotoxic effect.

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Effects of low-level laser therapy on mitochondrial respiration and nitrosyl complex content

et al. 2014

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Among the photochemical reactions responsible for therapeutic effects of low-power laser radiation, the photolysis of nitrosyl iron complexes of iron-containing proteins is of primary importance. The purpose of the present study was to compare the effects of blue laser radiation on the respiration rate and photolysis of nitrosyl complexes of iron-sulfur clusters (NO-FeS) in mitochondria, subjected to NO as well as the possibility of NO transfer from NO-FeS to hemoglobin. It was shown that mitochondrial respiration in State 3 (V3) and State 4 (V4), according to Chance, dramatically decreased in the presence of 3 mM NO, but laser radiation (λ = 442 nm, 30 J/cm(2)) restored the respiration rates virtually to the initial level. At the same time, electron paramagnetic resonance (EPR) spectra showed that laser irradiation decomposed nitrosyl complexes produced by the addition of NO to mitochondria. EPR signal of nitrosyl complexes of FeS-clusters, formed in the presence of 3 mM NO, was maximal in hypoxic mitochondria, and disappeared in a dose-dependent manner, almost completely at the irradiation dose 120 J/cm(2). EPR measurements showed that the addition of lysed erythrocytes to mitochondria decreased the amount of nitrosyl complexes in iron-sulfur clusters and produced the accumulation of NO-hemoglobin. On the other hand, the addition of lysed erythrocytes to mitochondria, preincubated with nitric oxide, restored mitochondrial respiration rates V3 and V4 to initial levels. We may conclude that there are two possible ways to destroy FeS nitrosyl complexes in mitochondria and recover mitochondrial respiration inhibited by NO: laser irradiation and ample supply of the compounds with high affinity to nitric oxide, including hemoglobin.

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Redox conversions of dinitrosyl iron complexes with natural thiol-containing ligands

Cited by 17 publications

References 22 publications

The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione

The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione

Physico-Chemistry of Dinitrosyl Iron Complexes as a Determinant of Their Biological Activity

Effects of low-level laser therapy on mitochondrial respiration and nitrosyl complex content

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