Summary: Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.

Top Publications

  1. Leimkuhler S, Rajagopalan K. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J Biol Chem. 2001;276:22024-31 pubmed
    ..form of MPT synthase can be activated by incubation with MoeB, Mg-ATP, l-cysteine, and one of the NifS-like sulfurtransferases, and the addition of precursor Z to the in vitro system gives rise to MPT formation...
  2. 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
    ..sulfur donor in vitro, and this apparent selectivity seems to be a unique property among the characterized sulfurtransferases. To investigate the basis of substrate recognition in RhdA, we replaced Thr-232 with either Ala or Lys...
  3. Pierrel F, Bjork G, Fontecave M, Atta M. Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein. J Biol Chem. 2002;277:13367-70 pubmed
    ..MiaB is the first and only tRNA modification enzyme known to contain an Fe-S cluster. ..
  4. Nagahara N, Okazaki T, Nishino T. Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directe. J Biol Chem. 1995;270:16230-5 pubmed
    ..The enzymes were expressed in Escherichia coli strain BL21 (DE3) with a T7 promoter system. The mutation of these residues decreases rhodanese activity and increases MST activity. ..
  5. Bui B, Florentin D, Fournier F, Ploux O, Mejean A, Marquet A. Biotin synthase mechanism: on the origin of sulphur. FEBS Lett. 1998;440:226-30 pubmed
    ..These enzymes were functional and when assayed in vitro produced labelled biotin containing about 65% of 34S. These data strongly support the hypothesis that the sulphur of biotin is derived from the (FeS) centre of the enzyme. ..
  6. Kispal G, Csere P, Prohl C, Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 1999;18:3981-9 pubmed
    ..Assembly of cellular Fe/S clusters constitutes an indispensable biosynthetic task of mitochondria with potential relevance for an iron-storage disease and the control of cellular iron uptake...
  7. Kambampati R, Lauhon C. Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. J Biol Chem. 2000;275:10727-30 pubmed
    ..coli tRNA(Phe). Together, these results suggest that ThiI is a recipient of S(0) from IscS and catalyzes the ultimate sulfur transfer step in the biosynthesis of s(4)U. ..
  8. Gibson K, Pelletier D, Turner I. Transfer of sulfur to biotin from biotin synthase (BioB protein). Biochem Biophys Res Commun. 1999;254:632-5 pubmed
    ..Mass spectrometry was consistent with covalent alteration of the protein in the assay. These results suggest that BioB protein is a reagent, not a catalyst. ..
  9. Waterman D, Ortiz Lombard a M, Fogg M, Koonin E, Antson A. Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain. J Mol Biol. 2006;356:97-110 pubmed publisher
    ..The inaccessibility of U8 in the canonical L-shaped form of tRNA, and the existence of a glycine-rich linker joining the catalytic and RNA-binding moieties of ThiI suggest that structural changes may occur in both molecules upon binding...

More Information


  1. Naamati A, Regev Rudzki N, Galperin S, Lill R, Pines O. Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55. J Biol Chem. 2009;284:30200-8 pubmed publisher
    ..Intriguingly, Icp55 protease (like its substrate Nfs1) appears to be dual distributed between the nucleus and mitochondria. ..
  2. Anton B, Saleh L, Benner J, Raleigh E, Kasif S, Roberts R. RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli. Proc Natl Acad Sci U S A. 2008;105:1826-31 pubmed publisher
    ..The initial results presented here constitute a bioinformatics-driven prediction with preliminary experimental validation that should serve as the starting point for several interesting lines of further inquiry. ..
  3. Lauhon C, Erwin W, Ton G. Substrate specificity for 4-thiouridine modification in Escherichia coli. J Biol Chem. 2004;279:23022-9 pubmed
    ..However, the secondary and tertiary structure restrictions appear sufficient to explain why s4U modification is limited in the cell to tRNA. ..
  4. Marquet A. Enzymology of carbon-sulfur bond formation. Curr Opin Chem Biol. 2001;5:541-9 pubmed
    ..This radical is produced by homolytic cleavage of a C-H bond by a deoxyadenosyl radical arising from the reduction of S-adenosylmethionine. ..
  5. Li J, Kogan M, Knight S, Pain D, Dancis A. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J Biol Chem. 1999;274:33025-34 pubmed
    ..These phenotypes include decreases in iron-sulfur protein activities coordinated with increases in cellular iron uptake and iron distribution to mitochondria. ..
  6. Nagahara N, Ito T, Kitamura H, Nishino T. 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;110:243-50 pubmed
    ..This immunocytochemical study also found that MST was localized in both mitochondria and cytoplasm. ..
  7. Leimkuhler S, Freuer A, Araujo J, Rajagopalan K, Mendel R. Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. J Biol Chem. 2003;278:26127-34 pubmed
  8. Mueller E, Palenchar P, Buck C. The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA. J Biol Chem. 2001;276:33588-95 pubmed
    ..We earlier noted the presence of a motif shared with sulfurtransferases, and we reported that the cysteine residue (Cys-456 of Escherichia coli ThiI) found in this motif is ..
  9. Pierrel F, Douki T, Fontecave M, Atta M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J Biol Chem. 2004;279:47555-63 pubmed
    ..The origin of the sulfur atom is discussed. ..
  10. Liu Y, Zhu X, Nakamura A, Orlando R, S ll D, Whitman W. Biosynthesis of 4-thiouridine in tRNA in the methanogenic archaeon Methanococcus maripaludis. J Biol Chem. 2012;287:36683-92 pubmed publisher
    ..Thus, methanogenic archaea developed a strategy for sulfur incorporation into s(4)U that differs from bacteria; this may be an adaptation to life in sulfide-rich environments...
  11. Adam A, Bornhovd C, Prokisch H, Neupert W, Hell K. The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J. 2006;25:174-83 pubmed
    ..In the absence of Isd11, Nfs1 is prone to aggregation. We propose that Isd11 acts together with Nfs1 in an early step in the biogenesis of Fe/S proteins. ..
  12. Nakamura T, Yamaguchi Y, Sano H. Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities. Eur J Biochem. 2000;267:5621-30 pubmed
    ..However, the mutation had no effect on levels of iron-sulfur enzyme activities, suggesting that MST1 is not directly involved in iron-sulfur cluster assembly. ..
  13. Nakai Y, Nakai M, Hayashi H. Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems. J Biol Chem. 2008;283:27469-76 pubmed publisher
    ..Taken together, our data indicate that the s(2) modification of cytosolic tRNAs is a more complex process that requires additional unidentified components. ..
  14. Mao G, Wang R, Guan Y, Liu Y, Zhang S. Sulfurtransferases 1 and 2 play essential roles in embryo and seed development in Arabidopsis thaliana. J Biol Chem. 2011;286:7548-57 pubmed publisher
    b>Sulfurtransferases (STRs) catalyze the transfer of a sulfur atom from a donor to a suitable acceptor molecule. The Arabidopsis thaliana genome encodes 20 putative STR proteins. The biological functions of most are unclear...
  15. Wiedemann N, Urzica E, Guiard B, Muller H, Lohaus C, Meyer H, et al. Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins. EMBO J. 2006;25:184-95 pubmed
    ..We conclude that Isd11 is an indispensable eukaryotic component of the mitochondrial machinery for biogenesis of Fe/S proteins. ..
  16. Layer G, Heinz D, Jahn D, Schubert W. Structure and function of radical SAM enzymes. Curr Opin Chem Biol. 2004;8:468-76 pubmed
    ..Remaining differences emphasize the plasticity of the protein scaffold in functionally accommodating 600 family members. ..
  17. Booker S, Cicchillo R, Grove T. Self-sacrifice in radical S-adenosylmethionine proteins. Curr Opin Chem Biol. 2007;11:543-52 pubmed
    ..This review will describe the characterization of three members of this class - biotin synthase, lipoyl synthase, and MiaB protein - each of which has been shown to cannibalize itself during turnover. ..
  18. Lee K, Saleh L, Anton B, Madinger C, Benner J, Iwig D, et al. Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily. Biochemistry. 2009;48:10162-74 pubmed publisher
    ..We discuss the possible requirement for an assembled ribosome for fully active RimO in vitro. Our findings are consistent with those of other enzymes that catalyze sulfur insertion, such as biotin synthase, lipoyl synthase, and MiaB. ..
  19. Reyda M, Fugate C, Jarrett J. A complex between biotin synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly. Biochemistry. 2009;48:10782-92 pubmed publisher
    ..We propose that HscA plays a role in facilitating the transfer of FeS clusters from IscU into the appropriate target apoproteins such as biotin synthase, perhaps by enhancing or prolonging the requisite protein-protein interaction. ..
  20. 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. ..
  21. 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). ..
  22. Ugulava N, Sacanell C, Jarrett J. Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion. Biochemistry. 2001;40:8352-8 pubmed
    ..We propose a mechanism for incorporation of sulfur into dethiobiotin in which a sulfur atom is oxidatively extracted from the [2Fe-2S](2+) cluster. ..
  23. Dahl J, Urban A, Bolte A, Sriyabhaya P, Donahue J, Nimtz M, et al. The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli. J Biol Chem. 2011;286:35801-12 pubmed publisher Moco biosynthesis in humans, the thiocarboxylation of the corresponding MoaD homolog involves two sulfurtransferases, an l-cysteine desulfurase, and a rhodanese-like protein, the rhodanese-like protein in E...
  24. Nakai Y, Umeda N, Suzuki T, Nakai M, Hayashi H, Watanabe K, et al. Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAs. J Biol Chem. 2004;279:12363-8 pubmed
    ..These results suggest that Nfs1p is involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mt-tRNAs and mcm(5)s(2)U in cy-tRNAs. ..
  25. Arragain S, Garcia Serres R, Blondin G, Douki T, Clemancey M, Latour J, et al. Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase. J Biol Chem. 2010;285:5792-801 pubmed publisher
    ..These biophysical results provide a foundation for understanding the mechanism of methylthioation by radical AdoMet enzymes in the MiaB/RimO family...
  26. Rajagopalan K. Biosynthesis and processing of the molybdenum cofactors. Biochem Soc Trans. 1997;25:757-61 pubmed
  27. Nagahara N, Sreeja V, Li Q, Shimizu T, Tsuchiya T, Fujii Kuriyama Y. A point mutation in a silencer module reduces the promoter activity for the human mercaptopyruvate sulfurtransferase. Biochim Biophys Acta. 2004;1680:176-84 pubmed
    ..A replacement of -391G to C lost the silencer function; on the other hand, a replacement of -394G to T or C, -393C to T or -392T to G markedly reduced the promoter activity. ..
  28. Stockdreher Y, Venceslau S, Josten M, Sahl H, Pereira I, Dahl C. Cytoplasmic sulfurtransferases in the purple sulfur bacterium Allochromatium vinosum: evidence for sulfur transfer from DsrEFH to DsrC. PLoS ONE. 2012;7:e40785 pubmed publisher well established for a number of biosynthetic pathways, evidence has only started to emerge that sulfurtransferases may also be major players in sulfur-based microbial energy metabolism...
  29. Kambampati R, Lauhon C. IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry. 1999;38:16561-8 pubmed
    ..Our identification of IscS as a tRNA sulfurtransferase provides support for this activity in vivo and further expands the role for NifS proteins as versatile sulfur-carrying enzymes. ..
  30. Shibuya N, Tanaka M, Yoshida M, Ogasawara Y, Togawa T, Ishii K, et al. 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain. Antioxid Redox Signal. 2009;11:703-14 pubmed publisher
    ..These data present a new perspective on H(2)S production and storage in the brain. ..
  31. Yi X, Maeda N. Endogenous production of lipoic acid is essential for mouse development. Mol Cell Biol. 2005;25:8387-92 pubmed
    ..65 g/kg of body weight) during pregnancy fails to prevent the prenatal deaths of homozygous embryos. Thus, endogenous LA synthesis is essential for developmental survival and cannot be replaced by LA in maternal tissues and blood. ..
  32. Mueller E, Palenchar P. Using genomic information to investigate the function of ThiI, an enzyme shared between thiamin and 4-thiouridine biosynthesis. Protein Sci. 1999;8:2424-7 pubmed
  33. 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. ..
  34. Bartels A, Mock H, Papenbrock J. Differential expression of Arabidopsis sulfurtransferases under various growth conditions. Plant Physiol Biochem. 2007;45:178-87 pubmed
    b>Sulfurtransferases (Str) comprise a group of enzymes widely distributed in archaea, eubacteria, and eukaryota which catalyse the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors...
  35. Hernandez H, Pierrel F, Elleingand E, Garcia Serres R, Huynh B, Johnson M, et al. MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry. 2007;46:5140-7 pubmed
  36. Krepinsky K, Leimkuhler S. Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs. FEBS J. 2007;274:2778-87 pubmed
    ..Furthermore, it could be shown that an MoeB homolog named MoeZ, where the dual CXXC zinc-binding motif of the MoeB domain is not present, arose independently several times during evolution. ..
  37. Esberg B, Leung H, Tsui H, Björk G, Winkler M. Identification of the miaB gene, involved in methylthiolation of isopentenylated A37 derivatives in the tRNA of Salmonella typhimurium and Escherichia coli. J Bacteriol. 1999;181:7256-65 pubmed
    ..Only a weak similarity to an AdoMet-binding site was found, favoring the idea that the MiaB protein is involved in the thiolation step and not in the methylating reaction of ms(2)i(o)(6)A37 formation. ..
  38. Mueller E, Buck C, Palenchar P, Barnhart L, Paulson J. Identification of a gene involved in the generation of 4-thiouridine in tRNA. Nucleic Acids Res. 1998;26:2606-10 pubmed
    ..This same gene, thiI , has recently been shown to play a role in thiamin biosynthesis. The purification and characteristics of the purified protein are also reported. ..
  39. Arragain S, Handelman S, Forouhar F, Wei F, Tomizawa K, Hunt J, et al. Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA. J Biol Chem. 2010;285:28425-33 pubmed publisher
    ..This work lays the foundation for elucidating the function of CDKAL1. ..
  40. Reiss J, Hahnewald R. Molybdenum cofactor deficiency: Mutations in GPHN, MOCS1, and MOCS2. Hum Mutat. 2011;32:10-8 pubmed publisher
    ..For type A deficiency an effective substitution therapy has been described recently. ..
  41. Tse Sum Bui B, Benda R, Schünemann V, Florentin D, Trautwein A, Marquet A. Fate of the (2Fe-2S)(2+) cluster of Escherichia coli biotin synthase during reaction: a Mössbauer characterization. Biochemistry. 2003;42:8791-8 pubmed
    ..This is consistent with the hypothesis that the reduced (4Fe-4S) cluster is involved in mediating the cleavage of AdoMet and that the (2Fe-2S)(2+) is the sulfur source for biotin. ..
  42. Cosper M, Jameson G, Hernandez H, Krebs C, Huynh B, Johnson M. Characterization of the cofactor composition of Escherichia coli biotin synthase. Biochemistry. 2004;43:2007-21 pubmed
    ..In addition, they provide a firm foundation for assessing cluster transformations that occur during turnover and the catalytic competence of the [2Fe-2S](2+) cluster as the immediate S-donor for biotin biosynthesis. ..
  43. Pierrel F, Hernandez H, Johnson M, Fontecave M, Atta M. MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase. J Biol Chem. 2003;278:29515-24 pubmed
    ..Finally, the expression of MiaBTm from T. maritima in an E. coli mutant strain lacking functional miaB gene allowed production of ms2i6A-37. These results provide further information on the enzymes involved in methylthiolation of tRNAs. ..
  44. Rudolph M, Wuebbens M, Rajagopalan K, Schindelin H. Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat Struct Biol. 2001;8:42-6 pubmed
    ..The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway. ..
  45. Gutzke G, Fischer B, Mendel R, Schwarz G. Thiocarboxylation of molybdopterin synthase provides evidence for the mechanism of dithiolene formation in metal-binding pterins. J Biol Chem. 2001;276:36268-74 pubmed
    ..A two-step reaction of MPT synthesis is proposed where the dithiolene is generated by two thiocarboxylates derived from a single tetrameric MPT synthase. ..
  46. Nagahara N, Katayama A. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis. J Biol Chem. 2005;280:34569-76 pubmed
    ..Thus the redox state regulates MST activity at the enzymatic level, and on the other hand, MST controls redox to maintain cellular redox homeostasis...
  47. Nagahara N, Yoshii T, Abe Y, Matsumura T. Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation. J Biol Chem. 2007;282:1561-9 pubmed
    ..E. coli C32S Trx, however, did not activate MST. Reduced Trx turns on a redox switch for the enzymatic activation of MST, which contributes to the maintenance of cellular redox homeostasis. ..
  48. Berkovitch F, Nicolet Y, Wan J, Jarrett J, Drennan C. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science. 2004;303:76-9 pubmed
    ..The structure places the substrates between the Fe4S4 cluster, essential for radical generation, and the Fe2S2 cluster, postulated to be the source of sulfur, with both clusters in unprecedented coordination environments. ..
  49. Bittner F, Oreb M, Mendel R. ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. J Biol Chem. 2001;276:40381-4 pubmed
    ..In a fully defined in vitro system, the purified protein was able to activate aldehyde oxidase by using L-cysteine as sulfur donor. Finally, we show that the expression of the aba3 gene is inducible by drought-stress. ..
  50. Nagahara N, Nirasawa T, Yoshii T, Niimura Y. Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase?. Antioxid Redox Signal. 2012;16:747-53 pubmed publisher
    ..Another sulfur acceptor substrate, cyanide, also converted these cysteines via cyanolysis. Thus, sulfur oxides are suggested to release in the redox cycle of persulfide of MST. ..
  51. Xiong L, Ishitani M, Lee H, Zhu J. The Arabidopsis LOS5/ABA3 locus encodes a molybdenum cofactor sulfurase and modulates cold stress- and osmotic stress-responsive gene expression. Plant Cell. 2001;13:2063-83 pubmed
    ..Our results show that LOS5/ABA3 is a key regulator of ABA biosynthesis, stress-responsive gene expression, and stress tolerance. ..
  52. Jarrett J. The novel structure and chemistry of iron-sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase. Arch Biochem Biophys. 2005;433:312-21 pubmed
  53. Lotierzo M, Tse Sum Bui B, Florentin D, Escalettes F, Marquet A. Biotin synthase mechanism: an overview. Biochem Soc Trans. 2005;33:820-3 pubmed
    ..When this compound was tested with a well-defined in vitro system, the same turnover of one and similar reaction rates were observed for DTB and DTBSH. We postulate that the same intermediate is formed from both substrates. ..
  54. Taylor A, Farrar C, Jarrett J. 9-Mercaptodethiobiotin is formed as a competent catalytic intermediate by Escherichia coli biotin synthase. Biochemistry. 2008;47:9309-17 pubmed publisher
    ..The retention of 9-mercaptodethiobiotin as a tightly bound intermediate is consistent with a mechanism involving the stepwise radical-mediated oxidative abstraction of sulfide from an iron-sulfur cluster. ..
  55. Marelja Z, Stöcklein W, Nimtz M, Leimkuhler S. A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J Biol Chem. 2008;283:25178-85 pubmed publisher
    ..Because MOCS3 was shown to be located in the cytosol, our results suggest that cytosolic Nfs1 has an important role in sulfur transfer for the biosynthesis of Moco. ..
  56. Mueller E. Trafficking in persulfides: delivering sulfur in biosynthetic pathways. Nat Chem Biol. 2006;2:185-94 pubmed
  57. Biederbick A, Stehling O, Rösser R, Niggemeyer B, Nakai Y, Elsässer H, et al. Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation. Mol Cell Biol. 2006;26:5675-87 pubmed
    ..The results have implications for the regulation of iron homeostasis by cytosolic iron regulatory protein 1. ..
  58. Broach R, Jarrett J. Role of the [2Fe-2S]2+ cluster in biotin synthase: mutagenesis of the atypical metal ligand arginine 260. Biochemistry. 2006;45:14166-74 pubmed
    ..Although we cannot exclude an as-yet-unidentified in vivo role in cluster repair or retention, we can conclude that Arg260 is not essential for the catalytic reaction of BS. ..
  59. Chowdhury M, Dosche C, Löhmannsröben H, Leimkuhler S. Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans. J Biol Chem. 2012;287:17297-307 pubmed publisher
    ..The cellular localization results showed that extension of the C terminus with an additional glycine of MOCS2A and URM1 altered the localization of MOCS3 from the cytosol to the nucleus. ..
  60. Yue Y, Zhang M, Zhang J, Duan L, Li Z. Arabidopsis LOS5/ABA3 overexpression in transgenic tobacco (Nicotiana tabacum cv. Xanthi-nc) results in enhanced drought tolerance. Plant Sci. 2011;181:405-11 pubmed publisher
    ..Thus, overexpression of LOS5 in transgenic tobacco can enhance drought tolerance. ..
  61. Shibuya N, Koike S, Tanaka M, Ishigami Yuasa M, Kimura Y, Ogasawara Y, et al. A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells. Nat Commun. 2013;4:1366 pubmed publisher
    ..This study presents a novel pathway of hydrogen sulphide production and provides a new therapeutic approach to deliver hydrogen sulphide to specific tissues. ..
  62. Williams M, Kana B, Mizrahi V. Functional analysis of molybdopterin biosynthesis in mycobacteria identifies a fused molybdopterin synthase in Mycobacterium tuberculosis. J Bacteriol. 2011;193:98-106 pubmed publisher
    ..By implicating multiple synthase-encoding homologs in MoCo biosynthesis, these results suggest that important cellular functions may be served by their expansion in M. tuberculosis. ..
  63. Zhang W, Urban A, Mihara H, Leimkuhler S, Kurihara T, Esaki N. IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. J Biol Chem. 2010;285:2302-8 pubmed publisher
    ..These findings indicate that IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of MPT synthase in MPT biosynthesis. ..
  64. Tanaka Y, Yamagata S, Kitago Y, Yamada Y, Chimnaronk S, Yao M, et al. Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand. RNA. 2009;15:1498-506 pubmed publisher
    ..Based on these results, a possible RNA binding mechanism of ThiI in which the N-terminal domain recognizes the acceptor-stem region and the C-terminal region causes a conformational change of RNA is proposed. ..
  65. Cicchillo R, Booker S. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J Am Chem Soc. 2005;127:2860-1 pubmed
    ..We show herein that the sulfur atoms in the lipoyl cofactor are derived from lipoyl synthase itself, and that each lipoyl synthase polypeptide contributes both of the sulfur atoms to the intact cofactor. ..
  66. Spallarossa A, Forlani F, Carpen A, Armirotti A, Pagani S, Bolognesi M, et al. The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: crystal structure of SseA from Escherichia coli. J Mol Biol. 2004;335:583-93 pubmed
    3-Mercaptopyruvate sulfurtransferases (MSTs) catalyze, in vitro, the transfer of a sulfur atom from substrate to cyanide, yielding pyruvate and thiocyanate as products...
  67. Leimkuhler S, Wuebbens M, Rajagopalan K. Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J Biol Chem. 2001;276:34695-701 pubmed
    ..All of these exhibited activity comparable to the wild type, with the exception of mutations in cysteine residues located in putative Zn-binding motifs. For these cysteines, loss of activity correlated with loss of metal binding. ..