<i>S</i>-Nitrosocysteine and Cystine from Reaction of Cysteine with Nitrous Acid. A Kinetic Investigation<sup>1</sup>

Grossi, Loris; Montevecchi, Pier Carlo

doi:10.1021/jo026154+

Cited by 43 publications

(50 citation statements)

References 12 publications

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“…Together, these two compounds represent 1-2% of the decomposed 1. The major pathway of decomposition of this S-nitrosothiol under our experimental conditions appears to be denitrosation since cystine is a major product in our reactions; it precipitates from the reaction mixture as a result of its poor water solubility as previously reported (5,13,14).…”

Section: Resultssupporting

confidence: 73%

Decomposition of S-Nitrosocysteine via S- to N-Transnitrosation

Peterson

Wagener

Sies

et al. 2007

Chem. Res. Toxicol.

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S-Nitrosothiols are thought to be important intermediates in nitric oxide signaling pathways. These compounds are unstable, in part, through their ability to donate NO. One model S-nitrosothiol, Snitrosocysteine is particularly unstable. Recently, it was proposed that this compound decomposed via intra-and intermolecular transfer of the NO group from the sulfur to the nitrogen to form Nnitrosocysteine. This primary nitrosamine is expected to rapidly rearrange to ultimately form a reactive diazonium ion intermediate. To test this hypothesis, we demonstrated that thiirane-2-carboxylic acid is formed during the decomposition of S-nitrosocysteine at neutral pH. Acrylic acid was another product of this reaction. These results indicate that a small but significant amount of Snitrosocysteine decomposes via S-to N-transnitrosation. The formation of a reactive intermediate in this process indicates the potential for this reaction to contribute to the toxicological properties of nitric oxide.

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Section: Resultssupporting

confidence: 73%

Decomposition of S-Nitrosocysteine via S- to N-Transnitrosation

Peterson

Wagener

Sies

et al. 2007

Chem. Res. Toxicol.

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“…Nonstandard chemical. S-Nitrosocysteine was synthesized and quantified as described previously (40,41).…”

Section: Bacterial Growth (I) Mediamentioning

confidence: 99%

Anaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella enterica and Escherichia coli

et al. 2017

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Salmonella enterica has two CyuR-activated enzymes that degrade cysteine, i.e., the aerobic CdsH and an unidentified anaerobic enzyme; Escherichia coli has only the latter. To identify the anaerobic enzyme, transcript profiling was performed for E. coli without cyuR and with overexpressed cyuR. Thirty-seven genes showed at least 5-fold changes in expression, and the cyuPA (formerly yhaOM) operon showed the greatest difference. Homology suggested that CyuP and CyuA represent a cysteine transporter and an iron-sulfur-containing cysteine desulfidase, respectively. E. coli and S. enterica ΔcyuA mutants grown with cysteine generated substantially less sulfide and had lower growth yields. Oxygen affected the CyuRdependent genes reciprocally; cyuP-lacZ expression was greater anaerobically, whereas cdsH-lacZ expression was greater aerobically. In E. coli and S. enterica, anaerobic cyuP expression required cyuR and cysteine and was induced by L-cysteine, D-cysteine, and a few sulfur-containing compounds. Loss of either CyuA or RidA, both of which contribute to cysteine degradation to pyruvate, increased cyuP-lacZ expression, which suggests that CyuA modulates intracellular cysteine concentrations. Phylogenetic analysis showed that CyuA homologs are present in obligate and facultative anaerobes, confirming an anaerobic function, and in archaeal methanogens and bacterial acetogens, suggesting an ancient origin. Our results show that CyuA is the major anaerobic cysteine-catabolizing enzyme in both E. coli and S. enterica, and it is proposed that anaerobic cysteine catabolism can contribute to coordination of sulfur assimilation and amino acid synthesis.IMPORTANCE Sulfur-containing compounds such as cysteine and sulfide are essential and reactive metabolites. Exogenous sulfur-containing compounds can alter the thiol landscape and intracellular redox reactions and are known to affect several cellular processes, including swarming motility, antibiotic sensitivity, and biofilm formation. Cysteine inhibits several enzymes of amino acid synthesis; therefore, increasing cysteine concentrations could increase the levels of the inhibited enzymes. This inhibition implies that control of intracellular cysteine levels, which is the immediate product of sulfide assimilation, can affect several pathways and coordinate metabolism. For these and other reasons, cysteine and sulfide concentrations must be controlled, and this work shows that cysteine catabolism contributes to this control.

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“…This protocol assumes an ∼85 % efficiency of the reaction (although published reports suggest an efficiency as high as ∼90 % [27]) and adds a sufficient concentration of sulfamate to remove all remaining NO 2 .…”

Section: Methodsmentioning

confidence: 99%

Biophysical and Proteomic Characterization Strategies for Cysteine Modifications in Ras GTPases

Hobbs

Gunawardena

Campbell

2013

Methods in Molecular Biology

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Cysteine is one of the most reactive amino acids and is modified by a number of oxidants. The reactivity of cysteines is dependent on the thiol pKa; however, measuring cysteine pKa values is nontrivial. Ras family GTPases have been shown to contain a free cysteine that is sensitive to oxidation, and free radical-mediated oxidation of this cysteine has been shown to be activating. Here, we present a new technique that allows for measuring cysteine pKa values using a fluorescent detection system with the molecule 4-fluoro-7-aminosulfonylbenzofurazan (ABD-F). In addition, we also describe how to generate several oxidants. Lastly, we describe several mass spectrometry-based experiments and the necessary adjustments to the experiments to detect cysteine oxidation.

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S-Nitrosocysteine and Cystine from Reaction of Cysteine with Nitrous Acid. A Kinetic Investigation¹

Cited by 43 publications

References 12 publications

Decomposition of S-Nitrosocysteine via S- to N-Transnitrosation

Decomposition of S-Nitrosocysteine via S- to N-Transnitrosation

Anaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella enterica and Escherichia coli

Biophysical and Proteomic Characterization Strategies for Cysteine Modifications in Ras GTPases

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S-Nitrosocysteine and Cystine from Reaction of Cysteine with Nitrous Acid. A Kinetic Investigation1

Cited by 43 publications

References 12 publications

Decomposition of S-Nitrosocysteine via S- to N-Transnitrosation

Decomposition of S-Nitrosocysteine via S- to N-Transnitrosation

Anaerobic Cysteine Degradation and Potential Metabolic Coordination in Salmonella enterica and Escherichia coli

Biophysical and Proteomic Characterization Strategies for Cysteine Modifications in Ras GTPases

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S-Nitrosocysteine and Cystine from Reaction of Cysteine with Nitrous Acid. A Kinetic Investigation¹