ライフサイエンスコーパス: persulfide

1 p to inactive Nfs1p induced formation of the persulfide.

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

3 introduced cysteine was modified to become a persulfide.

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

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

6 rcaptopyruvate to pyruvate and protein-bound persulfide.

7 h remains associated with the protein as Cys persulfide.

8 anslationally modified in vivo in the form a persulfide.

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

10 regulation favors the synthesis of H2S over persulfides.

11 modification of reactive cysteine thiols to persulfides.

12 hydrogen peroxide enhanced the formation of persulfides.

13 sulfur pools, which include hydrodisulfides/persulfides.

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

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

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

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

18 7.4 in the presence of various physiological persulfide acceptors: cysteine, dihydrolipoic acid, glut

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

75 Extensive persulfide formation is apparent in cysteine-containing

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

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

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

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

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

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

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

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

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

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

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

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

88 ys residue facilitates the generation of the persulfide group.

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

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

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

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

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

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

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

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

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

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

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

100 372 to form the Slr0077/SufS-bound cysteinyl persulfide intermediate and the second involving intermo

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

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

103 11p was inactive and did not form the [(35)S]persulfide intermediate from the substrate [(35)S]cystei

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

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

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

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

108 sulfur from cysteine via an enzyme cysteinyl persulfide intermediate.

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

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

111 y mechanism that recruits both disulfide and persulfide intermediates.

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

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

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

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

116 Similar persulfide ligands have been observed in vitro for sever

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

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

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

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

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

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

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

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

125 Such persulfide prodrugs can be used either as chemical tools

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

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

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

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

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

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

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

133 During aerobic persulfide reduction, rapid recycling of the persulfide

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

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

136 hydrodisulfide, thiosulfate, and glutathione persulfide, respectively.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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