NO-Group transfer (transnitrosation) between S-nitrosothiols and thiols. Part 2

Barnett, D. Jonathan; Ríos, Ana; Williams, D. Lyn H.

doi:10.1039/p29950001279

Cited by 61 publications

(35 citation statements)

References 6 publications

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“…It has been suggested that glyceraldehyde-3-phosphate dehydrogenase, protein kinase C, and glutathione peroxidase can all be inhibited by transnitrosation (10,11,15). Previous measurements of the kinetics and thermodynamics of transnitrosation have resorted to high concentrations of thiol and S-nitrosothiol in order to achieve sufficient optical absorbance (24,34,35). This procedure is subject to error, as the reductive reaction between thiol and nitrosothiol is favored at such high concentrations (4,23,35).…”

Section: Metal Ion-and Light-induced Decomposition Of S-nitrosothiols-mentioning

confidence: 99%

“…Previous determinations of the kinetic and thermodynamic parameters for these reactions have used extremely high concentrations of both thiol and nitrosothiol (0.5-10 mM) (24,34,35). The reasons for using high concentrations of S-nitrosothiols are: (i) most S-nitrosothiols have similar UV-vis spectra and (ii) the ⌬⑀ max for the transnitrosation reaction is less than 100 M Ϫ1 cm…”

Section: Effect Of Dmpo On Gssg Formation During Light-or Transition mentioning

confidence: 99%

“…S-Nitrosothiols have also been shown to form NO Ϫ , which under appropriate conditions can lead to the formation of either nitrous oxide (4,5,22) or peroxynitrite (4, 23). S-Nitrosothiols can also undergo nitrosonium (NO ϩ ) transfer to other cellular thiols by a process referred to as transnitrosation (24).In this study we have investigated the mechanism of decomposition and transnitrosation reactions of S-nitrosothiols using electron spin resonance (ESR), optical spectroscopy, high performance liquid chromatography (HPLC), and electrochemical methods. …”

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Mechanism of Nitric Oxide Release from S-Nitrosothiols

Singh

Hogg

Joseph

et al. 1996

Journal of Biological Chemistry

526

395

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S-NitrosothiolsS-Nitrosothiols are compounds with the generic structure of RSNO. Under appropriate conditions these compounds decompose to liberate nitric oxide ( ⅐ NO) and the corresponding disulfide (1). It has been suggested that the formation and decay of low molecular weight S-nitrosothiols, such as S-nitrosoglutathione (GSNO) 1 and S-nitrosocysteine (CySNO), may represent a mechanism for the storage or transport of ⅐ NO (2, 3). According to this proposal, S-nitrosothiols are synthesized chemically by reaction of ⅐ NO with thiol. Subsequently, these compounds are transported or diffuse to the site of action. Decomposition of the S-nitrosothiol then leads to ⅐ NO release and the corresponding biological effect. This hypothesis is mainly speculative and remains to be rigorously tested. Little is known about the reaction of ⅐ NO with glutathione (GSH) in vivo; however, the direct reaction of GSH with ⅐ NO does not generate GSNO but forms glutathione disulfide and nitroxyl anion (NO Ϫ ) (4, 5). GSNO is formed only if ⅐ NO is oxidized, by reaction with oxygen, to form ⅐ NO 2 and N 2 O 3 (6). As intracellular oxygen concentrations at the tissue level are in the range of 10 -20 M (7) and as the rate of ⅐ NO oxidation is proportional to the squared power of the ⅐ NO concentration (8), it is likely that the oxidation of ⅐ NO by oxygen in vivo is a slow and insignificant process (4). Evidence for the formation of S-nitrosothiols from endogenous ⅐ NO remains scarce (9). Nevertheless, nitrosylation of protein thiols has been implicated in the ⅐ NO-dependent regulation of many enzymes, including protein kinase C (10) and glyceraldehyde-3-phosphate dehydrogenase (11). It has been reported that normal human serum contains S-nitroso-serum albumin (12, 13) which has been proposed to act as an endogenous regulator of vessel tone (14).Although the physiological relevance of S-nitrosothiols remains to be established, these compounds have been used as donors of ⅐ NO (1, 15, 16). The most commonly employed compounds are GSNO and S-nitroso-N-acetyl-DL-penicillamine (SNAP) (Fig. 1A). Such compounds have been shown to have diverse and remarkable biological effects. For example, SNAP is a potent vasodilator (1) and low concentrations of GSNO have been shown to afford significant protection to the ischemic myocardium (17). It is generally assumed that S-nitrosothiols decompose by homolytic cleavage of the S-N bond (Reaction 1).This process generates ⅐ NO and a thiyl radical, RS ⅐ (18). However, this assumption has not been effectively tested under physiologically relevant conditions. It has been established that S-nitrosothiols are sensitive to both photolytic (19,20) and transition metal ion-dependent breakdown (21) but are stable in the presence of transition metal ion chelators in the dark. The biological activity of S-nitrosothiols may not be exclusively dictated by the release of ⅐ NO as the chemistry of these compounds is complex. S-Nitrosothiols have also been shown to form NO Ϫ , which under appropriate conditions can lead to...

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Section: Metal Ion-and Light-induced Decomposition Of S-nitrosothiols-mentioning

confidence: 99%

Section: Effect Of Dmpo On Gssg Formation During Light-or Transition mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Mechanism of Nitric Oxide Release from S-Nitrosothiols

Singh

Hogg

Joseph

et al. 1996

Journal of Biological Chemistry

526

395

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“…One such possible mechanism involves the attack of the nucleophilic thiol species at the sulfur atom of the S-nitrosothiol, resulting in the generation of nitroxyl (HNO) and the corresponding disulfide (3,121) RSNO ϩ RЈSH 3 RSSRЈ ϩ HNO (23) Another possible mechanism involves transnitrosation (i.e., transfer) of the equivalent of ϩ NO from one thiol to another (7,8). This does not directly result in the degradation of the S-nitrosothiol function but merely transfers it to another thiol RSNO ϩ RЈSH^RSH ϩ RЈSNO (24) The relative rates of these two processes are certainly a function of the accessibility of the attacking nucleophilic thiol to the two sites of attack as well as the relative electrophilicity of the sulfur and nitrogen atoms of the S-nitrosothiol.…”

Section: S-nitrosothiol Formation and Its Role In Redox Signalingmentioning

confidence: 99%

Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers

Forman¹,

Fukuto²,

Torrès³

2004

American Journal of Physiology-Cell Physiology

490

345

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. Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 287: C246 -C256, 2004; 10.1152/ ajpcell.00516.2003.-Except for the role of NO in the activation of guanylate cyclase, which is well established, the involvement of reactive oxygen species (ROS) and reactive nitrogen species (RNS) in signal transduction remains controversial, despite a large body of evidence suggestive of their participation in a variety of signaling pathways. Several problems have limited their acceptance as signaling molecules, with the major one being the difficulty in identifying the specific targets for each pathway and the chemical reactions supporting reversible oxidation of these signaling components, consistent with a second messenger role for ROS and RNS. Nevertheless, it has become clear that cysteine residues in the thiolate (i.e., ionized) form that are found in some proteins can be specific targets for reaction with H 2O2 and RNS. This review focuses on the chemistry of the reversible oxidation of those thiolates, with a particular emphasis on the critical thiolate found in protein tyrosine phosphatases as an example. hydrogen peroxide; thiolate; nitrosothiol; nitric oxide; signal transduction ALTHOUGH THE INVOLVEMENT OF FREE RADICALS in biology was assumed for many years to be restricted to damaging reactions, the discovery of the endogenous generation of NO in mammalian systems and the finding that this small, freely diffusing, chemically unique species participates in specific signal transduction pathways represented an important new paradigm and expanded views of the possible nature of cell communication and/or signaling processes. This novel role in signal transduction for ⅐NO and other reactive nitrogen species (RNS) now extends to reactive oxygen species (ROS) such as H 2 O 2 and is gaining greater acceptance. The skepticism that still exists about these molecules acting as second messengers in various signaling pathways may vanish with better understanding of their chemistry, particularly regarding the differences in reactivity at high concentrations (mainly associated with pathology and toxicology) from those at low concentrations generated under physiological conditions in response to stimuli. Several excellent reviews have been published regarding evidence supporting a role for ROS and RNS in signaling (26,32,75,82,87,117,119), and we (35, 36) previously described the general properties that define a second messenger and showed how ROS and RNS fit into this role. In this review, the main focus is on the chemistry that may provide specificity, a necessary property of second messengers that has remained the most elusive in the study of ROS and RNS. REACTIVE SPECIES AS SECOND MESSENGERSSecond messengers are generated at the time of receptor activation, are short-lived, and act specifically on effectors to transiently alter their activity. Indeed, ROS and RNS can be generated at the time of receptor activation and are short-lived, as a...

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