thiosulfate sulfurtransferase


Summary: An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC

Top Publications

  1. Ray W, Zeng G, Potters M, Mansuri A, Larson T. Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin. J Bacteriol. 2000;182:2277-84 pubmed for which sulfurtransferase activity has been confirmed. ..
  2. Cipollone R, Frangipani E, Tiburzi F, Imperi F, Ascenzi P, Visca P. Involvement of Pseudomonas aeruginosa rhodanese in protection from cyanide toxicity. Appl Environ Microbiol. 2007;73:390-8 pubmed publisher
    ..aeruginosa intrinsic resistance to cyanide, insofar as it provides the bacterium with a defense mechanism against endogenous cyanide toxicity, in addition to cyanide-resistant respiration...
  3. Cipollone R, Ascenzi P, Visca P. Common themes and variations in the rhodanese superfamily. IUBMB Life. 2007;59:51-9 pubmed
  4. Nagahara N, Ito T, Minami M. Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification. Histol Histopathol. 1999;14:1277-86 pubmed publisher
    ..Even in the same tissue, sensitivity to cyanide toxicity may differ according to the kind of cell. It is determined by a balance between the amount of proteins to be attacked and that of enzymes to defend. ..
  5. Mueller E. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol. 2006;2:185-94 pubmed
  6. Forlani F, Cereda A, Freuer A, Nimtz M, Leimkuhler S, Pagani S. The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form. FEBS Lett. 2005;579:6786-90 pubmed
    ..We were able to show the formation of a covalent complex between IscS and RhdA. By combining a time-course fluorescence assay and mass spectrometry analysis, we demonstrated the transfer of sulfur from E. coli IscS to RhdA...
  7. Adams H, Teertstra W, Koster M, Tommassen J. PspE (phage-shock protein E) of Escherichia coli is a rhodanese. FEBS Lett. 2002;518:173-6 pubmed
    ..8.1.1; rhodanese). Kinetic analysis revealed that catalysis occurs via a double displacement mechanism as described for other rhodaneses. The K(m)s for SSO3(2-) and CN- were 4.6 and 27 mM, respectively. ..
  8. Bordo D, Bork P. The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations. EMBO Rep. 2002;3:741-6 pubmed
    ..Furthermore, the frequently observed association of catalytically inactive rhodanese modules with other protein domains suggests a distinct regulatory role for these inactive domains, possibly in connection with signaling. ..
  9. Krueger K, Koch K, Jühling A, Tepel M, Scholze A. Low expression of thiosulfate sulfurtransferase (rhodanese) predicts mortality in hemodialysis patients. Clin Biochem. 2010;43:95-101 pubmed publisher
    To test the hypothesis that impaired expression of the thiosulfate sulfurtransferase rhodanese is associated with oxidative stress and may predict mortality in hemodialysis patients...

More Information


  1. Akinsiku O, Agboola F, Kuku A, Afolayan A. Physicochemical and kinetic characteristics of rhodanese from the liver of African catfish Clarias gariepinus Burchell in Asejire lake. Fish Physiol Biochem. 2010;36:573-586 pubmed publisher
    ..3 and 72.9 kcal/mol. Inhibition studies on the cRHD II enzyme showed that the activity of the enzyme was not affected by Mn(2+), Co(2+), Sn(2+), Ni(2+) and NH(4) (+), but Zn(2+) inhibited the enzyme considerably. ..
  2. Mizobata T, Kawagoe M, Hongo K, Nagai J, Kawata Y. Refolding of target proteins from a "rigid" mutant chaperonin demonstrates a minimal mechanism of chaperonin binding and release. J Biol Chem. 2000;275:25600-7 pubmed
    ..The possibility exists that some target proteins, although dependent on GroEL for improved refolding yields, are capable of refolding successfully by utilizing only portions of the entire mechanism provided by the chaperonins. ..
  3. Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, et al. A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese. Biol Chem. 2001;382:1245-52 pubmed
  4. Han W, Christen P. Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system. J Biol Chem. 2003;278:19038-43 pubmed
  5. Agboola F, Okonji R. Presence of rhodanese in the cytosolic fraction of the fruit bat (Eidolon helvum) liver. J Biochem Mol Biol. 2004;37:275-81 pubmed
    ..5 kcal/mol and 76.6 kcal/mol. Inhibition studies on the enzyme with a number of cations showed that Mg(2+), Mn(2+), Ca(2+), and Co(2+) did not affect the activity of the enzyme, but Hg(2+) and Ba(2+) inhibited the enzyme. ..
  6. Al Qarawi A, Mousa H, Ali B. Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds. Vet Res. 2001;32:63-70 pubmed
    ..The enzyme activity was equally distributed between the mitochondrial and cytosolic fractions in the liver and kidneys of camels, cattle and sheep. ..
  7. Cereda A, Carpen A, Picariello G, Tedeschi G, Pagani S. The lack of rhodanese RhdA affects the sensitivity of Azotobacter vinelandii to oxidative events. Biochem J. 2009;418:135-43 pubmed publisher
    ..vinelandii in maintaining the cellular redox balance was investigated by using an in vitro model system that demonstrated reversible chemical modifications in the highly reactive RhdA Cys(230) thiol. ..
  8. Schmitz J, Chowdhury M, Hänzelmann P, Nimtz M, Lee E, Schindelin H, et al. The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins. Biochemistry. 2008;47:6479-89 pubmed publisher
    ..The functional similarities between Uba4 and MOCS3 further demonstrate the evolutionary link between ATP-dependent protein conjugation and ATP-dependent cofactor sulfuration. ..
  9. Sani M, Gadacha W, Boughattas N, Reinberg A, Ben Attia M. Circadian and ultradian (12 h) rhythms of hepatic thiosulfate sulfurtransferase (rhodanese) activity in mice during the first two months of life. Chronobiol Int. 2006;23:551-63 pubmed
    b>Thiosulfate sulfurtransferase (TST) is an important 'enzyme of protection,' that accelerates the detoxification of cyanide, converting it into thiocyanate...
  10. Billaut Laden I, Allorge D, Crunelle Thibaut A, Rat E, Cauffiez C, Chevalier D, et al. Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme. Toxicology. 2006;225:1-11 pubmed
    Rhodanese or thiosulfate sulfurtransferase (TST) is a mitochondrial matrix enzyme that plays roles in cyanide detoxification, the formation of iron-sulfur proteins and the modification of sulfur-containing enzymes...
  11. Cereda A, Carpen A, Picariello G, Iriti M, Faoro F, Ferranti P, et al. Effects of the deficiency of the rhodanese-like protein RhdA in Azotobacter vinelandii. FEBS Lett. 2007;581:1625-30 pubmed
    ..The effect was dramatic on aconitase, in spite of comparable expression of aconitase polypeptides in both strains. By using a model system, we found that RhdA triggered protection from oxidants. ..
  12. Kawata Y, Kawagoe M, Hongo K, Miyazaki T, Higurashi T, Mizobata T, et al. Functional communications between the apical and equatorial domains of GroEL through the intermediate domain. Biochemistry. 1999;38:15731-40 pubmed
    ..These results point to a multitude of signals which govern the overall chaperonin mechanism. ..
  13. Nandi D, Westley J. Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese. Int J Biochem Cell Biol. 1998;30:973-7 pubmed
    ..The physiological compound alanine thiosulfonate also could serve as a donor substrate. In these systems, after a brief lag, inorganic sulfide accumulated as a final product. A formal mechanism in accord with all the results is proposed...
  14. Nagahara N, Nishino T. Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and site-directed mutagenesis. J Biol Chem. 1996;271:27395-401 pubmed
    ..On the other hand, Arg185, Arg247, and Lys248 of rat rhodanese are critical residues in determining substrate specificity for thiosulfate. ..
  15. Remelli W, Cereda A, Papenbrock J, Forlani F, Pagani S. The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance. Biol Chem. 2010;391:777-84 pubmed publisher
    ..vinelandii to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in A. vinelandii cells via redox reactions involving its cysteine thiol is discussed...
  16. Palenchar P, Buck C, Cheng H, Larson T, Mueller E. Evidence that ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J Biol Chem. 2000;275:8283-6 pubmed
    ..To accommodate this hypothesis, we propose a general mechanism for sulfur transfer in which the terminal sulfur of the persulfide first acts as a nucleophile and is then transferred as an equivalent of S(2-) rather than S(0). ..
  17. Miyazaki T, Yoshimi T, Furutsu Y, Hongo K, Mizobata T, Kanemori M, et al. GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle. J Biol Chem. 2002;277:50621-8 pubmed
    ..The behavior of GroEL C138W was reflected closely in its in vivo characteristics, demonstrating the importance of this conformational change to the overall activity of GroEL. ..
  18. Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S, Bolognesi M. The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. J Mol Biol. 2000;298:691-704 pubmed
    ..vinelandii rhodanese displays striking structural similarity to the active-site loop of the similarly folded catalytic domain of dual specific phosphatase Cdc25, suggesting a common evolutionary origin of the two enzyme families. ..
  19. Pagani S, Forlani F, Carpen A, Bordo D, Colnaghi R. Mutagenic analysis of Thr-232 in rhodanese from Azotobacter vinelandii highlighted the differences of this prokaryotic enzyme from the known sulfurtransferases. FEBS Lett. 2000;472:307-11 pubmed
    ..RhdA contains a unique sequence stretch around the catalytic cysteine, and the data here presented suggest a possible divergent physiological function of A. vinelandii sulfurtransferase. ..
  20. Pagani S, Galante Y. Interaction of rhodanese with mitochondrial NADH dehydrogenase. Biochim Biophys Acta. 1983;742:278-84 pubmed
    ..The results indicated that the [35S]sulfide was inserted in NADH dehydrogenase and appeared to constitute the structural basis for the increase in enzymic activity. ..
  21. Weissman J, Rye H, Fenton W, Beechem J, Horwich A. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell. 1996;84:481-90 pubmed
  22. Iciek M, Marcinek J, Mleczko U, Włodek L. Selective effects of diallyl disulfide, a sulfane sulfur precursor, in the liver and Ehrlich ascites tumor cells. Eur J Pharmacol. 2007;569:1-7 pubmed
    ..These data indicate that this compound is capable of acting efficiently and selectively only in the liver and can be used for hepatoprotection during chemotherapy. ..
  23. Wrobel M, Czubak J. Rhodanese (thiosulfate:cyanide sulfurtransferase) from frog Rana temporaria. J Chromatogr B Biomed Sci Appl. 2000;746:315-8 pubmed
  24. Trevino R, Hunt J, Horowitz P, Chirgwin J. Chinese hamster rhodanese cDNA: activity of the expressed protein is not blocked by a C-terminal extension. Protein Expr Purif. 1995;6:693-9 pubmed
    ..None of these substitutions occurs at residues suggested to play essential roles in catalysis or structural stabilization. ..
  25. Ogasawara Y, Lacourciere G, Stadtman T. Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system. Proc Natl Acad Sci U S A. 2001;98:9494-8 pubmed
    ..These results show that a selenium-bound rhodanese could be used as the selenium donor in the in vitro selenophosphate synthetase assay. ..
  26. Mouray E, Moutiez M, Girault S, Sergheraert C, Florent I, Grellier P. Biochemical properties and cellular localization of Plasmodium falciparum protein disulfide isomerase. Biochimie. 2007;89:337-46 pubmed
  27. van der Vaart A, Ma J, Karplus M. The unfolding action of GroEL on a protein substrate. Biophys J. 2004;87:562-73 pubmed
    ..The results of the simulation show that multidomain interactions play an essential role, in accord with experiments. Implications of the results for mutation experiments and for the action of GroEL are discussed. ..
  28. Sirur A, Best R. Effects of interactions with the GroEL cavity on protein folding rates. Biophys J. 2013;104:1098-106 pubmed publisher
    ..The origin of the slowdown appears to be stabilization--relative to repulsive confinement--of the unfolded state through binding to the cavity walls, rather than a reduction of the diffusion coefficient along the folding coordinate. ..
  29. Lewis J, Rhoades C, Gervasi P, Griffith W, Dahl A. The cyanide-metabolizing enzyme rhodanese in human nasal respiratory mucosa. Toxicol Appl Pharmacol. 1991;108:114-20 pubmed
    ..The Vmax/Km ratios for rhodanese from the nasal tissue of nonsmokers were consistently greater, thus suggesting the possibility of higher rates of cyanide metabolism in nonsmokers than in smokers. ..
  30. Laudenbach D, Ehrhardt D, Green L, Grossman A. Isolation and characterization of a sulfur-regulated gene encoding a periplasmically localized protein with sequence similarity to rhodanese. J Bacteriol. 1991;173:2751-60 pubmed
    ..The possible role of this protein in the transport of specific sulfur compounds is discussed. ..
  31. Wallen J, Mallett T, Boles W, Parsonage D, Furdui C, Karplus P, et al. Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking. Biochemistry. 2009;48:9650-67 pubmed publisher
    ..20 A bridge. ..
  32. Li H, Xia B, Jin C. 1H, 13C and 15N resonance assignments of rhodanese GlpE from Escherichia coli. Biomol NMR Assign. 2011;5:97-9 pubmed publisher
    ..Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of E. coli GlpE, which provides the basis for further structural, dynamic and functional studies of rhodaneses using NMR technique. ..
  33. Kawano Y, Onishi F, Shiroyama M, Miura M, Tanaka N, Oshiro S, et al. Improved fermentative L-cysteine overproduction by enhancing a newly identified thiosulfate assimilation pathway in Escherichia coli. Appl Microbiol Biotechnol. 2017;101:6879-6889 pubmed publisher
    ..The catalysis of thiosulfate to sulfite is at least partly mediated by thiosulfate sulfurtransferase (GlpE), because its overexpression could enhance cellular thiosulfate sulfurtransferase activity in ..
  34. Denu J, Dixon J. Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr Opin Chem Biol. 1998;2:633-41 pubmed
    ..In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms involving either intermolecular or intramolecular interactions, whereby inhibition is mediated by sterically blocking the active-site cleft. ..
  35. Cassanelli S, Moulis J. Sulfide is an efficient iron releasing agent for mammalian ferritins. Biochim Biophys Acta. 2001;1547:174-82 pubmed
    ..The results show that full reduction of sulfur into sulfide is needed to deplete iron from ferritin. These reactions suggest links between sulfur metabolism and intracellular iron homeostasis. ..
  36. Dubaquie Y, Looser R, Funfschilling U, Jeno P, Rospert S. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10. EMBO J. 1998;17:5868-76 pubmed
    ..We suggest that homologous substrate proteins have differential chaperonin requirements, indicating that hsp60 and hsp10 do not always act as a single functional unit in vivo. ..
  37. Zahn R, Buckle A, Perrett S, Johnson C, Corrales F, Golbik R, et al. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Proc Natl Acad Sci U S A. 1996;93:15024-9 pubmed
    ..The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions...
  38. Hatzfeld Y, Saito K. Evidence for the existence of rhodanese (thiosulfate:cyanide sulfurtransferase) in plants: preliminary characterization of two rhodanese cDNAs from Arabidopsis thaliana. FEBS Lett. 2000;470:147-50 pubmed
    ..AtRDH1 and AtRDH2 genes originated from the duplication of a large genomic region in chromosome 1 which took place before the appearance of the Arabidopsis genus. Our results confirm the existence of rhodanese in plants. ..
  39. Spallarossa A, Donahue J, Larson T, Bolognesi M, Bordo D. Escherichia coli GlpE is a prototype sulfurtransferase for the single-domain rhodanese homology superfamily. Structure. 2001;9:1117-25 pubmed
    ..Sequence searches through completed genomes indicate that GlpE can be considered to be the prototype structure for the ubiquitous single-domain rhodanese module. ..
  40. Eggo M, Warrack R, Ramasamy S, Langman M, Singh S. Is thiosulfate sulfurtransferase the colonic sulfide oxidase?. Dig Dis Sci. 2008;53:862 pubmed
  41. Mizobata T, Uemura T, Isaji K, Hirayama T, Hongo K, Kawata Y. Probing the functional mechanism of Escherichia coli GroEL using circular permutation. PLoS ONE. 2011;6:e26462 pubmed publisher
    ..We propose that circular permutation is a very versatile tool to probe chaperonin structure and function. ..
  42. Morton N, Beltram J, Carter R, Michailidou Z, Gorjanc G, McFadden C, et al. Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness. Nat Med. 2016;22:771-9 pubmed publisher
    ..mouse model, which has been selected for low adiposity over 60 generations, to identify mitochondrial thiosulfate sulfurtransferase (Tst; also known as rhodanese) as a candidate obesity-resistance gene with selectively increased ..
  43. Gajiwala K, Burley S. HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. J Mol Biol. 2000;295:605-12 pubmed publisher
    ..We suggest that HDEA may support chaperone-like functions during the extremely acidic conditions...
  44. Ybarra J, Bhattacharyya A, Panda M, Horowitz P. Active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-terminal domain and can be bound, inactivated, and reactivated by GroEL. J Biol Chem. 2003;278:1693-9 pubmed
    ..This conformation cannot as easily be achieved in the presence of the substrate, thiosulfate. ..
  45. Prat L, Maillard J, Rohrbach Brandt E, Holliger C. An unusual tandem-domain rhodanese harbouring two active sites identified in Desulfitobacterium hafniense. FEBS J. 2012;279:2754-67 pubmed publisher
    ..Our data suggest, however, that the presence of sulfide in the medium is responsible for the high expression of PhsE in Desulfitobacterium, where it could play a role in the sulfur homeostasis of the cell. ..
  46. Tayefi Nasrabadi H, Rahmani R. Partial purification and characterization of rhodanese from rainbow trout (Oncorhynchus mykiss) liver. ScientificWorldJournal. 2012;2012:648085 pubmed publisher
    ..Studies on the enzyme with a number of cations showed that the activity of the enzyme was not affected by Sn(2+), but Hg(2+), Ba(2+), Pb(2+), and Ca(2+) inhibited and Cu(2+) activated the enzyme with a concentration-dependent manner. ..
  47. Hall R, Henriksson K, Lewis S, Haller R, Kennaway N. Mitochondrial myopathy with succinate dehydrogenase and aconitase deficiency. Abnormalities of several iron-sulfur proteins. J Clin Invest. 1993;92:2660-6 pubmed
    ..5-kD subunit of complex II, compared to near normal levels of the 70-kD protein suggest a more generalized abnormality of the synthesis, import, processing, or assembly of a group of proteins containing iron-sulfur clusters. ..
  48. Eskandarzade N, Aminlari M, Golami S, Tavana M. Rhodanese activity in different tissues of the ostrich. Br Poult Sci. 2012;53:270-3 pubmed publisher
    ..5. The results suggest that the main organs harbouring high rhodanese activity in the ostrich are associated with sites likely to be required in rhodanese mediated cyanide detoxification. ..
  49. Sura P, Bronowicka Adamska P, Furtak E, Wróbel M. Effect of mercury ions on cysteine metabolism in Xenopus laevis tissues. Comp Biochem Physiol C Toxicol Pharmacol. 2011;154:180-6 pubmed publisher
  50. Polo C, Vazquez E, Caballero F, Gerez E, Battle A. Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation. Comp Biochem Physiol B. 1992;103:251-6 pubmed
  51. Petrikovics I, Budai M, Baskin S, Rockwood G, Childress J, Budai L, et al. Characterization of liposomal vesicles encapsulating rhodanese for cyanide antagonism. Drug Deliv. 2009;16:312-9 pubmed publisher
    ..Lipid composition was also optimized to achieve maximum encapsulation efficiency. ..
  52. Warner M, Lukose V, Lee K, Lopez K, H Sazinsky M, Crane E. Characterization of an NADH-dependent persulfide reductase from Shewanella loihica PV-4: implications for the mechanism of sulfur respiration via FAD-dependent enzymes. Biochemistry. 2011;50:194-206 pubmed
    ..On the basis of kinetic, titration, and structural data, a mechanism for the reduction of persulfides by Npsr is proposed...
  53. Natalello A, Mattoo R, Priya S, Sharma S, Goloubinoff P, Doglia S. Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates. J Mol Biol. 2013;425:1158-71 pubmed publisher
  54. Avvakumov G, Walker J, Xue S, Finerty P, MacKenzie F, Newman E, et al. Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). J Biol Chem. 2006;281:38061-70 pubmed
    ..The presence of a zinc ribbon subdomain near the ubiquitin binding site further suggests a polyubiquitin-specific binding site and a mechanism for substrate induced conformational changes. ..
  55. Gallo M, Melino S, Melis R, Paci M, Cicero D. Backbone NMR assignment of the 29.6 kDa rhodanese protein from Azotobacter vinelandii. J Biomol NMR. 2006;36 Suppl 1:73 pubmed
  56. Horowitz P, Butler M. Interactive intermediates are formed during the urea unfolding of rhodanese. J Biol Chem. 1993;268:2500-4 pubmed
  57. Kudlicki W, Coffman A, Kramer G, Hardesty B. Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. J Biol Chem. 1997;272:32206-10 pubmed
    ..The results lead to the conclusion that flexing of EF-Tu, especially as occurs between its open and closed conformations, is a major factor in its chaperone-like refolding activity. ..
  58. Cipollone R, Ascenzi P, Frangipani E, Visca P. Cyanide detoxification by recombinant bacterial rhodanese. Chemosphere. 2006;63:942-9 pubmed
    ..Our results indicate that cyanide detoxification by engineered E. coli cells is feasible under laboratory conditions, and suggest that microbial rhodaneses may contribute to cyanide transformation in natural environments. ..
  59. Wang H, Niu J, Chen P. [Analysis of the functions of wheat resistance-related genes by a transient expression system]. Yi Chuan Xue Bao. 2005;32:930-6 pubmed
  60. Tulsawani R, Debnath M, Pant S, Kumar O, Prakash A, Vijayaraghavan R, et al. Effect of sub-acute oral cyanide administration in rats: protective efficacy of alpha-ketoglutarate and sodium thiosulfate. Chem Biol Interact. 2005;156:1-12 pubmed
    ..This study indicates a promising role of alpha-KG and STS for the treatment of prolonged cyanide exposures. ..
  61. Hammen P, Weiner H. Structure of the cytosolic domain of TOM5, a mitochondrial import protein. FEBS Lett. 2000;468:101-4 pubmed
    ..The CD spectra show evidence of a helical structure that is invariant with pH. NOESY data revealed that TOM5 forms a stable helical core between E11 and R15 with a less structurally rigid helix extending to the C-terminus. ..
  62. Wrobel M, Sura P, Srebro Z. Sulfurtransferases and the content of cysteine, glutathione and sulfane sulfur in tissues of the frog Rana temporaria. Comp Biochem Physiol B Biochem Mol Biol. 2000;125:211-7 pubmed
    ..In the kidney, the possible participation of sulfane sulfur compounds in detoxification processes requires elucidation, similarly as in protection against cellular oxidative stress at extremely low levels of GSH. ..
  63. Chaudhry C, Farr G, Todd M, Rye H, Brunger A, Adams P, et al. Role of the gamma-phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energetics. EMBO J. 2003;22:4877-87 pubmed
    ..We discuss the likely basis of the ability of gamma-phosphate binding to convert preformed GroEL-GroES-ADP-polypeptide complexes into the folding-active state. ..
  64. Russell J, Weng L, Keim P, Heinrikson R. The covalent structure of bovine liver rhodanese. Isolation and partial structural analysis of cyanogen bromide fragements and the complete sequence of the enzyme. J Biol Chem. 1978;253:8102-8 pubmed
  65. Gliubich F, Berni R, Colapietro M, Barba L, Zanotti G. Structure of sulfur-substituted rhodanese at 1.36 A resolution. Acta Crystallogr D Biol Crystallogr. 1998;54:481-6 pubmed
    ..Only limited changes of the enzyme structure have been found as a result of the drastic change in the crystal medium. ..
  66. Furutani M, Ideno A, Iida T, Maruyama T. FK506 binding protein from a thermophilic archaeon, Methanococcus thermolithotrophicus, has chaperone-like activity in vitro. Biochemistry. 2000;39:453-62 pubmed
  67. Aussignargues C, Giuliani M, Infossi P, Lojou E, Guiral M, Giudici Orticoni M, et al. Rhodanese functions as sulfur supplier for key enzymes in sulfur energy metabolism. J Biol Chem. 2012;287:19936-48 pubmed publisher
    ..aeolicus. ..
  68. Wrobel M, Papla B. Rhodanese activity and total sulfur content in frog and mouse liver. Folia Histochem Cytobiol. 2000;38:11-7 pubmed
    ..The high total content of sulfur in the frog liver in autumn might be associated with sulfur storing for protein biosynthesis during the period of hibernation. ..
  69. Picton R, Eggo M, Merrill G, Langman M, Singh S. Mucosal protection against sulphide: importance of the enzyme rhodanese. Gut. 2002;50:201-5 pubmed
    ..A purified preparation of RHOD also detoxified H(2)S. RHOD, located in the submucosa and crypts of the colon, is the principal enzyme involved in H(2)S detoxication. TMT does not participate in the detoxication of H(2)S. ..
  70. Bischofberger P, Han W, Feifel B, Schönfeld H, Christen P. D-Peptides as inhibitors of the DnaK/DnaJ/GrpE chaperone system. J Biol Chem. 2003;278:19044-7 pubmed
    ..DnaK)m.substrate.DnaJn complexes. Apparently, simultaneous binding of DnaJ and DnaK to one and the same target polypeptide is essential for effective chaperone action. ..
  71. Tremmel D, Tropschug M. Neurospora crassa FKBP22 is a novel ER chaperone and functionally cooperates with BiP. J Mol Biol. 2007;369:55-68 pubmed
    ..These results suggest that BiP and FKBP22 form a folding helper complex with a high chaperoning capacity in the ER of Neurospora crassa. ..
  72. Naik S, Haque I, Degner N, Kornilayev B, Bomhoff G, Hodges J, et al. Identifying protein stabilizing ligands using GroEL. Biopolymers. 2010;93:237-51 pubmed publisher
    ..This development will provide a highly desirable tool for the pharmaceutical, academic, and medical professions. ..
  73. Cicero D, Melino S, Orsale M, Brancato G, Amadei A, Forlani F, et al. Structural rearrangements of the two domains of Azotobacter vinelandii rhodanese upon sulfane sulfur release: essential molecular dynamics, 15N NMR relaxation and deuterium exchange on the uniformly labeled protein. Int J Biol Macromol. 2003;33:193-201 pubmed
    ..On the contrary these results clearly indicate that upon the catalytic mechanism the two domains of the protein behave as a unique fold. ..
  74. Pantoja Uceda D, López Méndez B, Koshiba S, Kigawa T, Shirouzu M, Terada T, et al. NMR assignment of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana. J Biomol NMR. 2004;29:207-8 pubmed
  75. Noma A, Sakaguchi Y, Suzuki T. Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions. Nucleic Acids Res. 2009;37:1335-52 pubmed publisher
    ..The sulfur-flow of eukaryotic 2-thiouridine formation is distinct mechanism from the bacterial sulfur-relay system which is based on the persulfide chemistry. ..
  76. Sabelli R, Iorio E, De Martino A, Podo F, Ricci A, Viticchiè G, et al. Rhodanese-thioredoxin system and allyl sulfur compounds. FEBS J. 2008;275:3884-99 pubmed publisher
  77. Cornilescu G, Vinarov D, Tyler E, Markley J, Cornilescu C. Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana. Protein Sci. 2006;15:2836-41 pubmed
    ..Versions of this domain that lack the active site cysteine are found in other proteins, such as phosphatases, ubiquitin hydrolases, and sulfuryltransferases. ..
  78. Mayhew M, da Silva A, Martin J, Erdjument Bromage H, Tempst P, Hartl F. Protein folding in the central cavity of the GroEL-GroES chaperonin complex. Nature. 1996;379:420-6 pubmed
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