Kinetic study of the reaction between cystine and sulfide in alkaline solutions

Liu, David K.; Chang, Shih-Fu

doi:10.1139/v87-131

Cited by 21 publications

(20 citation statements)

References 4 publications

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“…As precedent, rate constants of (6.2 Ϯ 0.7) ϫ 10 Ϫ2 and 1.3 ϫ 10 Ϫ2 M Ϫ1 s Ϫ1 have been reported for the reaction of cystine with excess H 2 S in 50 mM borate buffer at pH 10.0 or NaOH 0.1 M, respectively (42). These values are lower, by factors of 15-70, than the pH-independent rate constant determined in this work, (9 Ϯ 2) ϫ 10…”

Section: Resultsmentioning

confidence: 76%

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Cuevasanta

Lange

Bonanata

et al. 2015

Journal of Biological Chemistry

295

344

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Background:Hydrogen sulfide (H 2 S) modulates physiological processes in mammals. Results: The reactivity of H 2 S toward disulfides (RSSR) and albumin sulfenic acid (RSOH) to form persulfides (RSSH) was assessed. Conclusion: H 2 S is less reactive than thiols. Persulfides have enhanced nucleophilicity. Significance: This kinetic study helps rationalize the contribution of the reactions with oxidized thiol derivatives to H 2 S biology.

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Section: Resultsmentioning

confidence: 76%

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Cuevasanta

Lange

Bonanata

et al. 2015

Journal of Biological Chemistry

295

344

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“…Disulfide-containing proteins including insulin, bovine serum albumin (BSA), ribonuclease, chymotrypsinogen A and ovalbumin all react with H 2 S to form hydrodisulfide. The apparent second order rate constants at 25°C were reported as 2.2 M −1 min −1 for cystamine, 0.35 M −1 min −1 for cystine (lower than that from [240]), 2.3 M −1 min −1 for denatured BSA and 4 M −1 min −1 for denatured insulin respectively. The reactions also occur at lower pH between 8 and 9.…”

Section: H2s Reaction With Thiol Derivatives (Or Thiol Reaction Wimentioning

confidence: 69%

“…The reaction is very reversible, the rate constants for the reaction and the reverse reaction were determined as 3.7 ± 0.4 M −1 min −1 and 5.5 ± 0.6 M −1 min −1 respectively at 25 °C, pH 10.0 and ionic strength 0.17 M [240]. A mixture of lipoate (the oxidized disulfide form of dihydrolipoate) and Na 2 S in 0.1 M sodium hydroxide (NaOH) also produces hydrodisulfide as measured by an absorption peak at 335 – 340 nm [241].…”

Section: H2s Reaction With Thiol Derivatives (Or Thiol Reaction Wimentioning

confidence: 99%

“…In the study of H 2 S reaction with cystine in basic solution (discussed in 6.1 ), the transsulfuration between cysteine and disulfane (HS 2 − ) was suggested [239]. The rate constants for the reaction and the reverse reaction were determined as 122 ± 20 M −1 min −1 and 6.1 ± 0.5 M −1 min −1 respectively at 25 °C, pH 10.0 and ionic strength 0.17 M [240]. In the case of GSH, a nucleophilic attack of GSH on the S 8 ring has also been suggested [275–277].…”

Section: H2s Reaction With Thiol Derivatives (Or Thiol Reaction Wimentioning

confidence: 99%

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Chemical foundations of hydrogen sulfide biology

2013

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Following nitric oxide (nitrogen monoxide) and carbon monoxide, hydrogen sulfide (or its newer systematic name sulfane, H2S) became the third small molecule that can be both toxic and beneficial depending on the concentration. In spite of its impressive therapeutic potential, the underlying mechanisms for its beneficial effects remain unclear. Any novel mechanism has to obey fundamental chemical principles. H2S chemistry was studied long before its biological relevance was discovered, however, with a few exceptions, these past works have received relatively little attention in the path of exploring the mechanistic conundrum of H2S biological functions. This review calls attention to the basic physical and chemical properties of H2S, focuses on the chemistry between H2S and its three potential biological targets: oxidants, metals and thiol derivatives, discusses the applications of these basics into H2S biology and methodology, and introduces the standard terminology to this youthful field.

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“…It has been demonstrated that H 2 S can drastically reduce metabolic demand (1). Similar to nitric oxide, H 2 S exerts protective effects on mitochondrial function and respiration (2). However, a conventional belief is that H 2 S is produced in the cytoplasm resulting from the cytosol localization of H 2 Sgenerating enzymes and is consumed through oxidation in mitochondria (3).…”

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confidence: 99%

Hydrogen sulfide (H ₂ S) metabolism in mitochondria and its regulatory role in energy production

Zhang²,

Wu³

et al. 2012

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

427

325

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Although many types of ancient bacteria and archea rely on hydrogen sulfide (H 2 S) for their energy production, eukaryotes generate ATP in an oxygen-dependent fashion. We hypothesize that endogenous H 2 S remains a regulator of energy production in mammalian cells under stress conditions, which enables the body to cope with energy demand when oxygen supply is insufficient. Cystathionine γ-lyase (CSE) is a major H 2 S-producing enzyme in the cardiovascular system that uses cysteine as the main substrate. Here we show that CSE is localized only in the cytosol, not in mitochondria, of vascular smooth-muscle cells (SMCs) under resting conditions, revealed by Western blot analysis and confocal microscopy of SMCs transfected with GFP-tagged CSE plasmid. After SMCs were exposed to A23187, thapsigargin, or tunicamycin, intracellular calcium level was increased, and CSE translocated from the cytosol to mitochondria. CSE was coimmunoprecipitated with translocase of the outer membrane 20 (Tom20) in mitochondrial membrane. Tom20 siRNA significantly inhibited mitochondrial translocation of CSE and mitochondrial H 2 S production. The cysteine level inside mitochondria is approximately three times that in the cytosol. Translocation of CSE to mitochondria metabolized cysteine, produced H 2 S inside mitochondria, and increased ATP production. Inhibition of CSE activity reversed A23187-stimulated mitochondrial ATP production. H 2 S improved mitochondrial ATP production in SMCs with hypoxia, which alone decreased ATP production. These results suggest that translocation of CSE to mitochondria on specific stress stimulations is a unique mechanism to promote H 2 S production inside mitochondria, which subsequently sustains mitochondrial ATP production under hypoxic conditions. mitochondrion | oxygen sensing | evolution | sulfur metabolism | phenylephrine M any photoautotrophic and chemoautotrophic bacteria and certain animals, such as the lugworm Arenicola marina, use sulfide as an energetic substrate. Mitochondria are the powerhouse of eukaryotic cells, where ATP is produced via oxidative phosphorylation. Considering mitochondria as the evolutionary trait of bacteria in eukaryotes, the metabolism of hydrogen sulfide (H 2 S) in mitochondria may serve as a means for energy supplementation. It has been demonstrated that H 2 S can drastically reduce metabolic demand (1). Similar to nitric oxide, H 2 S exerts protective effects on mitochondrial function and respiration (2). However, a conventional belief is that H 2 S is produced in the cytoplasm resulting from the cytosol localization of H 2 Sgenerating enzymes and is consumed through oxidation in mitochondria (3). It was recently demonstrated that mitochondria of human colon adenocarcinoma cells use sulfide as an energetic substrate at low micromolar concentrations, well below toxic levels (4). The foregoing observations call for reevaluation of the metabolism of H 2 S and its role in mitochondrial energization of eukaryotes. In the present study, we explored whether H 2 S can be prod...

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Kinetic study of the reaction between cystine and sulfide in alkaline solutions

Cited by 21 publications

References 4 publications

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Chemical foundations of hydrogen sulfide biology

Hydrogen sulfide (H ₂ S) metabolism in mitochondria and its regulatory role in energy production

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Kinetic study of the reaction between cystine and sulfide in alkaline solutions

Cited by 21 publications

References 4 publications

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

Chemical foundations of hydrogen sulfide biology

Hydrogen sulfide (H 2 S) metabolism in mitochondria and its regulatory role in energy production

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Product

Resources

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Hydrogen sulfide (H ₂ S) metabolism in mitochondria and its regulatory role in energy production