ライフサイエンスコーパス: persulfide

1 h remains associated with the protein as Cys persulfide.

2 anslationally modified in vivo in the form a persulfide.

3 d higher K(m) for the substrate, glutathione persulfide.

4 p to inactive Nfs1p induced formation of the persulfide.

5 cysteine-PLP complex to form free l-cysteine persulfide.

6 omposing to generate N-acetyl cysteine (NAC) persulfide.

7 introduced cysteine was modified to become a persulfide.

8 ucture of IVD is consistent with that of CoA persulfide.

9 , resulting in the production of alanine and persulfide.

10 e, which rapidly collapses to form a defined persulfide.

11 rcaptopyruvate to pyruvate and protein-bound persulfide.

12 s potential to generate low-molecular-weight persulfides.

13 form of [2Fe-2S](2+) cluster-bound cysteine persulfides.

14 ransfer between IscS and FdhD in the form of persulfides.

15 ion of cysteine residues to produce reactive persulfides.

16 regulation favors the synthesis of H2S over persulfides.

17 modification of reactive cysteine thiols to persulfides.

18 hydrogen peroxide enhanced the formation of persulfides.

19 sulfur pools, which include hydrodisulfides/persulfides.

20 emical basis of the biological properties of persulfides.

21 ditional sulfur gave the corresponding boron persulfide, a NHC-stabilized boradithiirane.

22 ition to sulfite, glutathione functions as a persulfide acceptor for human SQR and that rhodanese pre

23 oxin is likely to be the major physiological persulfide acceptor for MST.

24 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glut

25 s(-1)), indicating that the substituents in persulfides affect properties to a lesser extent than in

26 The enzyme-persulfide.Ala complex dissociates rapidly with a K(d) o

27 ned as a dead-end complex between the enzyme-persulfide and a second l-cysteine, which adds to the co

28 e PP-loop pyrophosphatase domain to generate persulfide and disulfide intermediates for sulfur transf

29 oduced sulfane sulfur, including glutathione persulfide and inorganic polysulfide, produced from eith

30 echanism for the stabilization of the enzyme persulfide and perselenide intermediates during catalysi

31 for the generation of H(2)S and glutathione persulfide and reactivation of an oxidatively modified f

32 t determination of the pK(a) of a biological persulfide and the first examination of the alpha effect

33 nthesis and reactivity of mononuclear Zn(2+) persulfide and thioselenide complexes from a unified syn

34 xidoreductase (SQR), which converts H2S to a persulfide and transfers electrons to coenzyme Q via a f

35 ing the fundamental difference between alkyl persulfides and alkyl thiolates.

36 labile and sulfane sulfur species, including persulfides and polysulfides.

37 in part by sulfane sulfur species, including persulfides and polysulfides.

38 We cover the chemical biology of persulfides and the chemical probes for detecting them.

39 directly investigate the reactivity between persulfides and thiols to answer these questions.

40 termediate, as a nucleophile to form an NFS1 persulfide, and as a sulfur delivery agent to generate a

41 r copper (CsoR) plus CstR, which responds to persulfide, and formaldehyde-responsive FrmR.

42 romiscuous and reduces a range of disulfide, persulfide, and polysulfide compounds.

43 ve sulfur species, such as hydrogen sulfide, persulfides, and polysulfides, have recently emerged as

44 rid mechanisms often invoke the formation of persulfides, and so a survey of binary and ternary mater

45 Sulfide and persulfide are chemically different and one might expect

46 sulfide and with peroxynitrite revealed that persulfides are better nucleophiles than thiols, which i

47 d approaches highlight how the properties of persulfides are directly impacted by local environments,

48 Moreover, persulfides are electrophilic at both sulfur atoms, and

49 MS also demonstrates that multiple cysteine persulfides are formed on O(2) exposure of [4Fe-4S](2+)-

50 s are required for anion oxidation, in which persulfides are formed.

51 Although persulfides are stronger nucleophiles than their thiol c

52 ct evidence for the formation of thioredoxin persulfide as a product of this reaction.

53 sulted in concomitant production of cysteine persulfide as cluster ligands.

54 the formation and stability of the cysteine persulfide as well as the specificity of sulfur transfer

55 The persulfide bond appears to be essential for either the a

56 ke activity by both binding to and mediating persulfide bond cleavage of sulfur-loaded IscS, the sulf

57 rates thioredoxin-like activity by mediating persulfide bond cleavage of sulfur-loaded NifS (an IscS-

58 nally competent reducing agent for cysteinyl persulfide bond cleavage, releasing inorganic sulfide fo

59 a cysteine residue recently found to form a persulfide bond with the C-cluster were characterized.

60 alanine with the concomitant formation of a persulfide bond with the catalytic cysteine residue, thu

61 structural changes, such as the formation of persulfide bonds.

62 sulfur species like H(2)S, polysulfides, and persulfides, both carbonyl sulfide (COS) and carbon disu

63 substrate cysteine is the source of the Nfs1 persulfide, but this step is independent of frataxin and

64 me could be subsequently induced to form the persulfide by addition of Isd11p.

65 teine to generate alanine and an active-site persulfide (C(364)-S-S(-)).

66 ective in mediating sulfur signaling because persulfide can directly modify protein cysteine residue.

67 steric bulk or electron withdrawal near the persulfide can shunt persulfide reactivity through the t

68 nucleophiles than their thiol counterparts, persulfides can also act as electrophiles in their neutr

69 an be used either as chemical tools to study persulfide chemistry and biology or for future developme

70 cofactor of the resting enzyme suggest that persulfide cleavage by dithiols occurs by prior formatio

71 f the observed first-order rate constant for persulfide cleavage by DTT on the concentration of the d

72 similarity of the maximum rate constant for persulfide cleavage by DTT to k(cat) suggests that persu

73 intermediate, and it has been suggested that persulfide cleavage is the rate-limiting step for cataly

74 fide cleavage by DTT to k(cat) suggests that persulfide cleavage is, in fact, primarily rate-determin

75 xyethyl)phosphine (TCEP), the most efficient persulfide cleaver identified, is used as the reducing c

76 (II)(TPA)(OTf)](+) afforded the eta(1)-alkyl persulfide complex [Co(II)(TPA)(SS(t)Bu)](+) (2), which

77 We also prepared a mononuclear Zn(2+) persulfide complex and probed differences in persulfide

78 ed the formation of a novel, transient U(VI)-persulfide complex as an intermediate species during the

79 a simple synthon to access rare metal alkyl persulfide complexes and to investigate the reactivity o

80 f MPT in vitro but only in the presence of a persulfide-containing sulfurtransferase such as IscS, cy

81 d products, including a [3Fe-3S] cluster and persulfide-coordinated [2Fe-2S] clusters [[2Fe-2S](S) n

82 NR can also be regenerated from the cysteine persulfide-coordinated [2Fe-2S](2+) cluster by anaerobic

83 The thioredoxin persulfide could serve a biological function such as the

84 e reducing intracellular milieu, glutathione persulfide could serve as a persulfide donor for protein

85 taining pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermedia

86 tion pathway enzymes can synthesize cysteine persulfide (Cys-SSH) from cystine and H2S from cysteine

87 Cysteine-persulfide (Cys-SSH) is a cysteine whose sulfhydryl grou

88 mV), allows cyanide to displace the cysteine persulfide (CysS(-)) ligand to the active site heme.

89 contains a haem with unprecedented cysteine persulfide (cysteine sulfane) coordination.

90 nthesis in vivo without detectably affecting persulfide delivery and suggest that additional assays m

91 To enhance persulfide delivery to cells, we conjugated the SOPD mot

92 o substrates are NAD(P)H and di-, poly-, and persulfide derivatives of coenzyme A, although polysulfi

93 Mutations in the persulfide dioxgenase, i.e. ETHE1, result in ethylmaloni

94 tabolism via sulfide quinone oxidoreductase, persulfide dioxygenase (ETHE1), rhodanese, and sulfite o

95 ain sulfide:quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO) genes.

96 ch comprises sulfide quinone oxidoreductase, persulfide dioxygenase (PDO), rhodanese, and sulfite oxi

97 acterization and kinetic properties of human persulfide dioxygenase and describe the biochemical pena

98 FFE-NH(2) ) to make a superoxide-responsive, persulfide-donating peptide (SOPD-Pep).

99 ding from these insights, we use a synthetic persulfide donor and an N-iodoacetyl l-tyrosine methyl e

100 However, the source of the persulfide donor and whether its relationship to H2S is

101 ieu, glutathione persulfide could serve as a persulfide donor for protein persulfidation, a posttrans

102 Termed SOPD-NAC, this persulfide donor reacts specifically with O(2) (.-) , de

103 haracterization, and in vivo evaluation of a persulfide donor that releases N-acetyl cysteine persulf

104 as a reactive oxygen species (ROS)-activated persulfide donor.

105 have developed one- and two-photon-activated persulfide donors based on an o-nitrobenzyl (ONB) photot

106 are well established, and various H(2)S and persulfide donors have been developed.

107 we examined the cytotoxicity of synthesized persulfide donors on HeLa cells and the cytoprotective a

108 is hindered because of the lack of efficient persulfide donors.

109 the proposed nucleophilicity enhancement of persulfides due to the alpha-effect, and providing new i

110 esidue of rhodanese that transiently forms a persulfide during catalysis.

111 and propose that Cys-456 transiently forms a persulfide during catalysis.

112 cysteine desulfurase IscS, which forms a Cys persulfide enzyme adduct from free Cys; and ThiI, which

113 ere proposed to transfer sulfur via cysteine persulfide enzyme adducts, whereas the reaction mechanis

114 transfer in which the terminal sulfur of the persulfide first acts as a nucleophile and is then trans

115 ione polysulfide, containing glutathione and persulfide, for iron-sulfur cluster assembly in the cyto

116 f L-cysteine can bind to the cofactor in the persulfide form of CD-0387 explain why several CDs are s

117 The boron persulfide formally inserted phenyl acetylene into the B

118 Our results give light on the mechanisms of persulfide formation and provide quantitative evidence f

119 our study contribute to the understanding of persulfide formation and reactivity.

120 eosides (s(4)U and mnm(5)s(2)U) that require persulfide formation and transfer.

121 beta-latch does not affect the chemistry of persulfide formation but does protect it from undesired

122 Extensive persulfide formation is apparent in cysteine-containing

123 tes its formation with C-S bond cleavage and persulfide formation, is supported by its failure to dev

124 nd the active site cysteine in proximity for persulfide formation.

125 the tRNA uridine and transfers sulfur from a persulfide formed on the protein.

126 propose a regulatory mechanism for the Nfs1 persulfide-forming activity.

127 The Ser mutant of the persulfide-forming Cys316 was essentially inactive and d

128 The structure shows that the persulfide-forming cysteine occurs at the tip of a loop

129 onstant of 10 s(-1), the slowest step in the persulfide-forming half-reaction.

130 a model acceptor protein, we showed that the persulfide-forming MSTs catalyze roGFP2 oxidation and mo

131 fE binds near the SufS active site to accept persulfide from Cys-364.

132 ssory protein SufE work together to mobilize persulfide from L-cysteine, which is then donated to the

133 ed with concomitant formation of glutathione persulfide, glutathione disulfide, and H2S.

134 y both inorganic tetrasulfide and an organic persulfide, glutathione persulfide, to yield a mixture o

135 The formation of a persulfide group (-SSH) on cysteine residues has gained

136 These results suggest that a persulfide group (containing a sulfane sulfur) is the pr

137 ys residue facilitates the generation of the persulfide group.

138 o demonstrate that the larger V1 Hb can form persulfide groups on its linker chains, a mechanism that

139 he oxygen-dependent oxidation of glutathione persulfide (GSSH) to give persulfite and glutathione.

140 transfer of sulfane sulfur from glutathione persulfide (GSSH) to sulfite generating thiosulfate and

141 ides with glutathione to produce glutathione persulfide (GSSH).

142 acidity, and nucleophilicity of glutathione persulfide (GSSH/GSS(-)), the derivative of the abundant

143 sulfide oxidation being: H2S --> glutathione persulfide --> sulfite --> sulfate, than with a more con

144 ate pure hydrogen sulfide (H(2) S), hydrogen persulfide (H(2) S(2) ), and N-acetyl-l-cysteine persulf

145 Hydrogen persulfide (H(2)S(2)) is an important sulfur-containing

146 Both SOPD-NAC and SOPD-Pep delivered persulfides/H(2) S to H9C2 cardiomyocytes and lowered RO

147 A general strategy of delivering hydrogen persulfide (H2S2) is described herein.

148 The persulfides had higher reactivity with monobromobimane t

149 Persulfides have been considered as potential signaling

150 the physiological substrate of ATM3 contains persulfide in addition to glutathione.

151 than a monothiol, which must react with the persulfide in bimolecular fashion.

152 fane sulfur (S(0)) in the form of a cysteine persulfide in its active site.

153 and sulfane sulfur in the form of a cysteine persulfide in the active site of the enzyme.

154 ), we examined the activities of sulfide and persulfide in vitro and in vivo.

155 le of H(2)S rather than low molecular weight persulfides in regulating SQOR.

156 PROTEIN1 (ETHE1) catalyzes the oxidation of persulfides in the mitochondrial matrix and is essential

157 ility to enhance intracellular production of persulfides, including GSSH, CysSSH, H(2)S(2), H(2)S(3),

158 d from an irreversible inactivation by their persulfide intermediate and subsequent reactivation by t

159 372 to form the Slr0077/SufS-bound cysteinyl persulfide intermediate and the second involving intermo

160 rate binding to PLP, formation of a covalent persulfide intermediate at the active site cysteine, and

161 l change, thereby promoting formation of the persulfide intermediate at the active site cysteine.

162 11p was inactive and did not form the [(35)S]persulfide intermediate from the substrate [(35)S]cystei

163 e kinetics and mechanisms of cleavage of the persulfide intermediate in Slr0387 (CD-0387), a sequence

164 chanism of formation of the enzyme cysteinyl persulfide intermediate in the reaction of a cysteine de

165 he sulfane sulfur from an SQR-bound cysteine persulfide intermediate to a small-molecule acceptor is

166 tant TCEP to react with the active-site C364-persulfide intermediate to complete the SufS catalytic c

167 ransfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as

168 l as a cosubstrate to reductively cleave the persulfide intermediate, and it has been suggested that

169 sulfur from cysteine via an enzyme cysteinyl persulfide intermediate.

170 eine to form alanine and an enzyme cysteinyl persulfide intermediate.

171 by an esterase to generate a "hydroxymethyl persulfide" intermediate, which rapidly collapses to for

172 H(2)S oxidation pathway that form catalytic persulfide intermediates, sulfide quinone oxidoreductase

173 y mechanism that recruits both disulfide and persulfide intermediates.

174 se of 4-thiouridine synthesis, purified IscS-persulfide is able to provide sulfur for in vitro s(2)U

175 Alkylation of the Zn(2+) persulfide is considerably faster than the Zn(2+) thiola

176 e pyridoxal phosphate-containing site, and a persulfide is formed on the active site cysteine in a ma

177 The SufS persulfide is protected from external oxidants/reductant

178 lfide oxidation pathway in which glutathione persulfide is the first intermediate formed.

179 The persulfide is then transferred to the scaffold Isu, wher

180 critical active site residue rather than the persulfide itself.

181 ine structure (EXAFS) modeling showed that a persulfide ligand was coordinated in the equatorial plan

182 Similar persulfide ligands have been observed in vitro for sever

183 to function as a shuttle protein that uses a persulfide linkage to a single invariant cysteine residu

184 These unprecedented, aberrant persulfide linkages may shed new light upon the mechanis

185 ed to the H(2) S prodrug in vivo, indicating persulfide might represent a better therapeutic paradigm

186 hes indicate that PA1006 protein serves as a persulfide-modified protein that is critical for molybde

187 or ischemic stroke, by integrating H(2)S and persulfide moieties directly into NBP's carbonyl groups.

188 y of binary and ternary materials containing persulfide moieties is presented to provide context for

189 materials that show thermodynamically stable persulfide moieties.

190 MtAhpE-SOH reacted with H(2)S, forming a persulfide (MtAhpE-SSH) detectable by mass spectrometry.

191 gger, which releases the biologically active persulfide (N-acetyl l-cysteine persulfide, NAC-SSH) in

192 ulfide (H(2) S(2) ), and N-acetyl-l-cysteine persulfide (N-CysSSH), we examined the activities of sul

193 ulfide donor that releases N-acetyl cysteine persulfide (NAC-SSH) in response to the prokaryote-speci

194 cally active persulfide (N-acetyl l-cysteine persulfide, NAC-SSH) in a spatiotemporal manner.

195 persulfide complex and probed differences in persulfide nucleophilicity when compared to the parent t

196 substrate to generate alanine and a covalent persulfide on an active site cysteine residue.

197 ctivity of ABA3 by reducing the intermediate persulfide on its catalytic cysteine, thereby accelerati

198 tantly, we have identified the (35)S-labeled persulfide on the NFS1 cysteine desulfurase as a genuine

199 to several metabolic pathways in the form of persulfides on specific cysteine residues of an acceptor

200 ations show that the oxidation of sulfide to persulfide only occurs when a neighboring vacancy is pre

201 f the mitochondrion-localized, GSH-dependent persulfide oxygenase ETHE1, suggesting that the physiolo

202 difies cysteine residues in proteins to form persulfides (P-SSH).

203 w of the active site of this enzyme in apo-, persulfide, perselenide, and selenocysteine-bound interm

204 The different persulfides presented similar pK(a) values (4.6-6.3) and

205 Under near physiological conditions, the persulfide prodrug can be activated by an esterase to ge

206 Persulfide prodrugs also possess a reduced level of toxi

207 Such persulfide prodrugs can be used either as chemical tools

208 Using the persulfide prodrugs developed in this study, the reactiv

209 Persulfide prodrugs exhibited increased activities compa

210 depending on the organism, which accepts the persulfide product and delivers it to downstream partner

211 ological processes, can be released from the persulfide product of the MPST reaction.

212 Investigating CARS-dependent persulfide production may thus clarify aberrant redox si

213 ontributes to a fundamental understanding of persulfide properties and their modulation by protein en

214 ridine biosynthesis by the enzyme ThiI using persulfide (R-S-S-H) chemistry.

215 r another disulfide to form a small-molecule persulfide (R-S-S-H).

216 olecules that have catenated sulfur atoms as persulfides (R-SSH) and polysulfides (R-SS(n)H).

217 Persulfides (R-SSH) have been hypothesized as potent red

218 the specific properties that control whether persulfides react through the H(2)S-releasing or transpe

219 ron withdrawal near the persulfide can shunt persulfide reactivity through the transpersulfidation pa

220 lpha-effect, and providing new insights into persulfide reactivity when coordinated to metals.

221 domain on C-terminal NFU binding to NifS and persulfide reductase activity is also examined.

222 Only the C-terminal domain is required for persulfide reductase activity, while complex formation o

223 gent and found that Mo-bpy undergoes anionic persulfide reduction to form the tetragonal Mo(VI) compl

224 During aerobic persulfide reduction, rapid recycling of the persulfide

225 ity, whereas Yah1 supplies electrons for the persulfide reduction.

226 Next, we have demonstrated the detection of persulfide release both qualitatively and quantitatively

227 treated with control compounds incapable of persulfide release or in animals treated with Na(2) S.

228 We suggest that this persulfide replaced ThiI by donating sulfur to the thiam

229 erve one Fe2S2 cluster bound by two cysteine persulfide residues.

230 hydrodisulfide, thiosulfate, and glutathione persulfide, respectively.

231 racterization, and fundamental reactivity of persulfide (RSS(-)), perselenide (RSeSe(-)), thioselenid

232 (L(MW)SH) and protein (PrSH) thiols to form persulfides (RSS(-)) and polysulfides (RS(S)(n)S(-)) for

233 Persulfides (RSS(-)) and thioselenides (RSSe(-)) play im

234 Persulfides (RSS(-)) are ubiquitous source of sulfides (

235 ound that reacts with O(2) (.-) to release a persulfide (RSSH), a type of reactive sulfur species rel

236 Reactive sulfane sulfur species such as persulfides (RSSH) and H(2)S(2) are important redox regu

237 Persulfides (RSSH) are biologically important reactive s

238 H2S with disulfides and sulfenic acids yield persulfides (RSSH), recently identified post-translation

239 l modification of cysteine residues (RSH) to persulfides (RSSH).

240 Persulfides (RSSH/RSS(-)) participate in sulfur metaboli

241 Persulfides (RSSH/RSS(-)) participate in sulfur traffick

242 sed kinetic profiling strategy, suggest that persulfide selectivity is determined by structural frust

243 CstR is a persulfide-sensing member of the functionally diverse co

244 terial pathogen Acinetobacter baumannii as a persulfide sensor.

245 sing cluster and readily reacts with organic persulfides, showing no reactivity or DNA dissociation f

246 A strategy to deliver a well-defined persulfide species in a biological medium is described.

247 and as a sulfur delivery agent to generate a persulfide species on the Fe-S scaffold protein ISCU2.

248 Our identification of a new, labile U(VI)-persulfide species under environmentally relevant condit

249 erved, likely due to intermediate uranyl(VI)-persulfide species.

250 A persulfide-specific chemoselective proteomics approach w

251 persulfide reduction, rapid recycling of the persulfide substrate was observed, which is proposed to

252 says suggest that R119A EcSufE can receive a persulfide, suggesting the residue may function in a rel

253 The release of persulfide sulfur also requires GTP and NADH, probably m

254 ata indicate that a loss of PA1006 protein's persulfide sulfur and a reduced availability of molybden

255 We found that the release of persulfide sulfur from NFS1 requires iron, showing that

256 ed two pathways that involve the transfer of persulfide sulfur in humans, molybdenum cofactor biosynt

257 In physiological settings, the persulfide sulfur is released from NFS1 and transferred

258 ducing reagents, suggesting that transfer of persulfide sulfur occurs to cysteinyl groups of IscU.

259 alkylation of SufU support the occurrence of persulfide sulfur transfer steps in the mechanism of Suf

260 ors that serve as efficient acceptors of the persulfide sulfur.

261 on of thiosulfate to sulfite and glutathione persulfide; sulfur transfer in the reverse direction was

262 hese enzymes serve as the principal cysteine persulfide synthases in vivo.

263 mma-cystathionase (CSE) and for homocysteine persulfide synthesis from homocystine by CSE only.

264 may generate a protein-bound polysulfide or persulfide that serves as the immediate S donor for biot

265 Due to the inherent instability of persulfides, their chemistry is understudied.

266 sulfidation from a bulky penicillamine-based persulfide to a cysteine-based thiol, which, to the best

267 logical function such as the transfer of the persulfide to a target protein or the sequestered releas

268 re chemically different and one might expect persulfide to be more effective in mediating sulfur sign

269 s the transpersulfurase, SufE, to accept the persulfide to complete the SufS catalytic cycle.

270 equent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide.

271 cess H(2)S would directly react with protein persulfides to generate H(2)S(2) and reduce the persulfi

272 sulfides to generate H(2)S(2) and reduce the persulfides to thiols.

273 lfide and an organic persulfide, glutathione persulfide, to yield a mixture of Cys31-Cys60' interprot

274 usively with oxidized sulfur species such as persulfides, to yield a tetrasulfide bridge that inhibit

275 urases to understand mechanisms of protected persulfide transfer across protein interfaces.

276 close approach SufS-SufE complex to promote persulfide transfer.

277 leophilicity of several low molecular weight persulfides using the alkylating agent, monobromobimane.

278 en S-methyl methanethiosulfonate (MMTS) with persulfide was unambiguously demonstrated.

279 r the flow of sulfide via SQR to glutathione persulfide, which is then partitioned to thiosulfate or

280 lfides and sulfenic acids) and thereby forms persulfides, which are plausible transducers of the H(2)

281 iols such as dithiothreitol (DTT) cleave the persulfide with approximately 100-fold greater efficienc

282 l reactivity differences between sulfide and persulfide would translate into pharmacological differen