H2S and its role in redox signaling

doi:10.1016/j.bbapap.2014.01.002

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Volume 1844, Issue 8, August 2014, Pages 1355-1366

https://doi.org/10.1016/j.bbapap.2014.01.002 Get rights and content

Highlights

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H₂S, a signaling molecule is produced and cleared by the sulfur metabolic network.
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The mechanism and regulation of H₂S action remain largely unknown.
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The chemical properties of H₂S and its varied physiological effects are discussed.

Abstract

Hydrogen sulfide (H₂S) has emerged as an important gaseous signaling molecule that is produced endogenously by enzymes in the sulfur metabolic network. H₂S exerts its effects on multiple physiological processes important under both normal and pathological conditions. These functions include neuromodulation, regulation of blood pressure and cardiac function, inflammation, cellular energetics and apoptosis. Despite the recognition of its biological importance and its beneficial effects, the mechanism of H₂S action and the regulation of its tissue levels remain unclear in part owing to its chemical and physical properties that render handling and analysis challenging. Furthermore, the multitude of potential H₂S effects has made it difficult to dissect its signaling mechanism and to identify specific targets. In this review, we focus on H₂S metabolism and provide an overview of the recent literature that sheds some light on its mechanism of action in cellular redox signaling in health and disease. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.

Introduction

Sulfur-based chemistry is exploited by nature for maintaining cellular redox homeostasis, for redox-based signaling and for neutralizing reactive oxygen and nitrogen species. Reactive cysteine residues in the proteome are important constituents of redox signaling pathways. Reversible changes in the oxidation state of cysteines allow them to function as redox switches in multiple signaling pathways [1] and these residues are often targets of modifications. Additionally, transition metal centers with sulfur ligands can participate in redox-signaling pathways and function as biological redox sensors. Some key messengers used for communication through these redox hotspots are reactive oxygen species (ROS) and reactive nitrogen species (RNS) along with the gaseous signaling molecules such as CO, NO and H₂S. Recognition of H₂S as a signaling molecule in mammals took longer than NO and CO perhaps due to its long reputation as an environmental toxin and the prevailing view that it was primarily relevant to microbial metabolism. However, since the first report of a physiological role for endogenously produced H₂S in mammals [2], there has been an explosion in the literature of its varied biological effects (Fig. 1). Among the signaling mechanisms invoked for H₂S, cysteine persulfidation is the one that is most commonly cited [3]. However, the technical problems associated with existing methods for the detection of proteomic persulfidation raise concerns about the validity of the identified targets [4] in addition to raising questions about how target specificity is achieved. The chemical versatility of H₂S and the multiplicity of its reported targets suggest that additional mechanisms might be involved in H₂S signaling.

Fundamental gaps in our understanding of how intracellular H₂S is regulated hamper in turn, our understanding of its mechanism of action and target selectivity. At least three enzymes, cystathionine β-synthase (CBS), cystathione γ-lyase (CSE) [5], [6], and 3-mercaptopyruvate sulfurtransferase (MST) [7], [8], contribute to H₂S production (Fig. 2a). Housekeeping enzymes produce H₂S and it is not known whether signaling by H₂S as with NO and CO, can be regulated by increased enzymatic synthesis. It is also not known how H₂S biogenesis is selectively regulated relative to the canonical transsulfuration reactions catalyzed by CBS and CSE [9], [10]. The low tissue concentration of H₂S is a product of both the H₂S biogenesis and oxidation fluxes [11].

Section snippets

H₂S production

H₂S is produced endogenously from cysteine and homocysteine via various reactions catalyzed by CBS and CSE [5], [6] and from 3-mercaptopyruvate in a reaction catalyzed by MST [7], [8] (Fig. 2a). 3-Mercaptopyruvate is derived via a transamination reaction between cysteine and α-ketoglutarate catalyzed by cysteine aminotransferase (CAT), which is identical to aspartate aminotransferase [12]. MST catalyzes the desulfuration of 3-mercaptopyruvate generating an MST-bound persulfide at an active site

Chemical properties of H₂S

H₂S is a weak acid and readily ionizes in aqueous solution with pK_a1 and pK_a2 values of 6.9 and > 12 respectively [49]. Therefore at physiological pH, approximately two thirds of total H₂S is in the anionic sulfide (HS⁻) form. Further ionization to S²⁻ requires alkaline conditions. Hence, the concentration of the sulfide dianion is negligible under cellular conditions. H₂S is lipophilic and can freely diffuse through membranes [50]. While the electronic configuration of sulfur is similar to that

Protein persulfidation

An increasing number of reports suggest the importance of protein persulfidation in H₂S-based signaling [77]. In principle, persulfidation can occur by one of at least three mechanisms: (i) nucleophilic attack of a sulfide anion on an oxidized cysteine residue, e.g. sulfenic acid, S-nitrosyl or disulfide, (ii) via transsulfuration from an existing persulfide carried by a small molecule like GSSH or a protein, or (iii) by attack of a cysteine thiol on H₂S₂ [78] (Fig. 2a,b) or polysulfide [79].

Vasorelaxation

H₂S functions as an endothelial-derived hyperpolarizing factor (EDHF) and its vasorelaxant activity is ascribed primarily to activation of K_ATP channels [18], [62], [85], [86], [87], [124]. The effect of H₂S on relaxation of blood vessels is sensitive to the presence of K_ATP channel inhibitors and believed to involve direct channel activation by H₂S [85], [86], [124], [125]. Alternatively, an indirect mechanism can be considered as inhibition of cytochrome c oxidase results in reduced ATP

Summary

As fast-moving as the field of H₂S biochemistry has become, the pace is tempered by the many gaps in our understanding of the molecular mechanisms underlying sulfide oxidation, H₂S homeostasis and H₂S signaling targets. These gaps in knowledge also represent opportunities for moving the field forward. The controversies surrounding the sometimes dichotomous effects of H₂S (e.g. it is both pro- and anti-inflammatory) highlight the problems associated with interpreting studies performed with a

References (216)

T. Chiku et al.
H2S biogenesis by human cystathionine gamma-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia
J. Biol. Chem.
(2009)
S. Singh et al.
Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H₂S biogenesis via alternative trans-sulfuration reactions
J. Biol. Chem.
(2009)
A. Meister et al.
Enzymatic desulfuration of beta-mercaptopyruvate to pyruvate
J. Biol. Chem.
(1954)
P.W. Beatty et al.
Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes
Arch. Biochem. Biophys.
(1980)
G.D. Westrop et al.
The mercaptopyruvate sulfurtransferase of Trichomonas vaginalis links cysteine catabolism to the production of thioredoxin persulfide
J. Biol. Chem.
(2009)
P.K. Yadav et al.
Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase
J. Biol. Chem.
(2013)
S. Singh et al.
PLP-dependent H₂S biogenesis
Biochim. Biophys. Acta
(2011)
V. Vitvitsky et al.
Taurine biosynthesis by neurons and astrocytes
J. Biol. Chem.
(2011)
M.H. Stipanuk et al.
Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism
J. Nutr.
(2006)
P.K. Yadav et al.
Allosteric communication between the pyridoxal 5′-phosphate (PLP) and heme sites in the H2S generator human cystathionine beta-synthase
J. Biol. Chem.
(2012)

C.G. Curtis et al.

Detoxication of sodium 35 S-sulphide in the rat

Biochem. Pharmacol.

(1972)

T.C. Bartholomew et al.

Oxidation of sodium sulphide by rat liver, lungs and kidney

Biochem. Pharmacol.

(1980)

M.M. Cherney et al.

Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification

J. Mol. Biol.

(2010)

T.P. Singer et al.

Intermediary metabolism of L-cysteinesulfinic acid in animal tissues

Arch. Biochem. Biophys.

(1956)

D. Yonezawa et al.

A protective role of hydrogen sulfide against oxidative stress in rat gastric mucosal epithelium

Toxicology

(2007)

Z. Fu et al.

Hydrogen sulfide protects rat lung from ischemia-reperfusion injury

Life Sci.

(2008)

M. Whiteman et al.

Hydrogen sulphide: a novel inhibitor of hypochlorous acid-mediated oxidative damage in the brain?

Biochem. Biophys. Res. Commun.

(2005)

M. Whiteman et al.

Evidence for the formation of a novel nitrosothiol from the gaseous mediators nitric oxide and hydrogen sulphide

Biochem. Biophys. Res. Commun.

(2006)

S. Carballal et al.

Reactivity of hydrogen sulfide with peroxynitrite and other oxidants of biological interest

Free Radic. Biol. Med.

(2011)

P. Wardman et al.

Kinetic factors that control the fate of thiyl radicals in cells

Methods Enzymol.

(1995)

N.E. Francoleon et al.

The reaction of H(2)S with oxidized thiols: generation of persulfides and implications to H(2)S biology

Arch. Biochem. Biophys.

(2011)

S.A. Everett et al.

Perthiols as antioxidants: radical-scavenging and prooxidative mechanisms

Methods Enzymol.

(1995)

V. Massey et al.

On the mechanism of inactivation of xanthine oxidase by cyanide

J. Biol. Chem.

(1970)

U. Branzoli et al.

Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase

J. Biol. Chem.

(1974)

J.L. Hargrove

Persulfide generated from L-cysteine inactivates tyrosine aminotransferase. Requirement for a protein with cysteine oxidase activity and gamma-cystathionase

J. Biol. Chem.

(1988)

N. Sen et al.

Hydrogen sulfide-linked sulfhydration of NF-kappaB mediates its antiapoptotic actions

Mol. Cell

(2012)

R. Hosoki et al.

The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide

Biochem. Biophys. Res. Commun.

(1997)

L. Li et al.

Actions and interactions of nitric oxide, carbon monoxide and hydrogen sulphide in the cardiovascular system and in inflammation—a tale of three gases!

Pharmacol. Ther.

(2009)

A. Fago et al.

Integrating nitric oxide, nitrite and hydrogen sulfide signaling in the physiological adaptations to hypoxia: a comparative approach

Comp. Biochem. Physiol. A Mol. Integr. Physiol.

(2012)

P.B. Massion et al.

Regulation of the mammalian heart function by nitric oxide

Comp. Biochem. Physiol. A Mol. Integr. Physiol.

(2005)

N. Brandes et al.

Thiol-based redox switches in eukaryotic proteins

Antioxid. Redox Signal.

(2009)

K. Abe et al.

The possible role of hydrogen sulfide as an endogenous neuromodulator

J. Neurosci.

(1996)

B.D. Paul et al.

H(2)S signalling through protein sulfhydration and beyond

Nat. Rev. Mol. Cell Biol.

(2012)

J. Pan et al.

Persulfide reactivity in the detection of protein S-sulfhydration

ACS Chem. Biol.

(2013)

N. Shibuya et al.

Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide

J. Biochem.

(2009)

E. Mosharov et al.

The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes

Biochemistry

(2000)

V. Vitvitsky et al.

High turnover rates for hydrogen sulfide allow for rapid regulation of its tissue concentrations

Antioxid. Redox Signal.

(2012)

T. Ubuka et al.

Purification and characterization of mitochondrial cysteine aminotransferase from rat liver

Physiol. Chem. Phys.

(1978)

Y. Mikami et al.

Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide

Biochem. J.

(2011)

O. Kabil et al.

The quantitative significance of the transsulfuration enzymes for H2S production in murine tissues

Antioxid. Redox Signal.

(2011)

Y. Ogasawara et al.

Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat

Biol. Pharm. Bull.

(1994)

G. Yang et al.

H₂S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase

Science

(2008)

N. Nagahara et al.

Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis

Histochem. Cell Biol.

(1998)

N. Shibuya et al.

3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain

Antioxid. Redox Signal.

(2009)

O. Kabil et al.

Enzymology of H₂S biogenesis, decay and signaling

Antioxid. Redox Signal.

(2013)

N. Motl et al.

Enzymology of hydrogen sulfide turnover

V. Vitvitsky et al.

Perturbations in homocysteine-linked redox homeostasis in a murine model for hyperhomocysteinemia

Am. J. Physiol. Regul. Integr. Comp. Physiol.

(2004)

N. Tateishi et al.

Studies on the regulation of glutathione level in rat liver

J. Biochem.

(1974)

I. Ueki et al.

Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase

Am. J. Physiol. Endocrinol. Metab.

(2012)

J. Furne et al.

Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values

Am. J. Physiol. Regul. Integr. Comp. Physiol.

(2008)

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Citation Excerpt :
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^☆: This article is part of a Special Issue entitled: Thiol-Based Redox Processes.

^☆☆: This work was supported in part by a grant from the National Institutes of Health (HL58984 to R.B.) and the American Heart Association (13SDG17070096 to O.K.).

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ReviewH2S and its role in redox signaling☆,☆☆

Highlights

Abstract

Introduction

Section snippets

H2S production

Chemical properties of H2S

Protein persulfidation

Vasorelaxation

Summary

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Arch. Biochem. Biophys.

J. Biol. Chem.

J. Biol. Chem.

Biochim. Biophys. Acta

J. Biol. Chem.

J. Nutr.

J. Biol. Chem.

Biochem. Pharmacol.

Biochem. Pharmacol.

J. Mol. Biol.

Arch. Biochem. Biophys.

Toxicology

Life Sci.

Biochem. Biophys. Res. Commun.

Biochem. Biophys. Res. Commun.

Free Radic. Biol. Med.

Methods Enzymol.

Arch. Biochem. Biophys.

Methods Enzymol.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

Mol. Cell

Biochem. Biophys. Res. Commun.

Pharmacol. Ther.

Comp. Biochem. Physiol. A Mol. Integr. Physiol.

Comp. Biochem. Physiol. A Mol. Integr. Physiol.

Thiol-based redox switches in eukaryotic proteins

Antioxid. Redox Signal.

The possible role of hydrogen sulfide as an endogenous neuromodulator

J. Neurosci.

H(2)S signalling through protein sulfhydration and beyond

Nat. Rev. Mol. Cell Biol.

Persulfide reactivity in the detection of protein S-sulfhydration

ACS Chem. Biol.

Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide

J. Biochem.

The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes

Biochemistry

High turnover rates for hydrogen sulfide allow for rapid regulation of its tissue concentrations

Antioxid. Redox Signal.

Purification and characterization of mitochondrial cysteine aminotransferase from rat liver

Physiol. Chem. Phys.

Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide

Biochem. J.

The quantitative significance of the transsulfuration enzymes for H2S production in murine tissues

Antioxid. Redox Signal.

Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat

Biol. Pharm. Bull.

H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase

Science

Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis

Histochem. Cell Biol.

3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain

Antioxid. Redox Signal.

Enzymology of H2S biogenesis, decay and signaling

Antioxid. Redox Signal.

Enzymology of hydrogen sulfide turnover

Perturbations in homocysteine-linked redox homeostasis in a murine model for hyperhomocysteinemia

Am. J. Physiol. Regul. Integr. Comp. Physiol.

Studies on the regulation of glutathione level in rat liver

J. Biochem.

Extrahepatic tissues compensate for loss of hepatic taurine synthesis in mice with liver-specific knockout of cysteine dioxygenase

Am. J. Physiol. Endocrinol. Metab.

Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values

Am. J. Physiol. Regul. Integr. Comp. Physiol.

Review
H₂S and its role in redox signaling☆,☆☆

H₂S production

Chemical properties of H₂S

H₂S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase

Enzymology of H₂S biogenesis, decay and signaling