MetaCyc Pathway: thiosulfate disproportionation III (rhodanese)
Traceable author statement to experimental support

Enzyme View:

Pathway diagram: thiosulfate disproportionation III (rhodanese)

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationInorganic Nutrients MetabolismSulfur Compounds MetabolismThiosulfate Disproportionation

Some taxa known to possess this pathway include : Azotobacter vinelandii, Bos taurus, Escherichia coli K-12 substr. MG1655, Mammalia, Starkeya novella

Expected Taxonomic Range: Bacteria , Eukaryota

General Background

The inorganic sulfur compound thiosulfate contains two sulfur atoms: a sulfone-sulfur (oxidation state +V), and a sulfane-sulfur (oxidation state -I). At low pH thiosulfate decomposes spontaneously to sulfite and elemental sulfur [Hashwa72]. At neutral pH the compound is relatively stable, but several types of bacteria can catalyze its disproportionation in a process in which thiosulfate serves as both an electron donor and an electron acceptor.

Several types of enzymes have been described that are able to catalyze the disproportionation of thiosulfate. These enzymes have been differentiated based on the nature of the electron donor: some enzymes require thiols for this purpose, others utilize organic electron donors such as pyruvate, as well as molecular hydrogen in the presence of a hydrogenase, and some enzymes have only been active in vitro when coupled to cyanide. These three classes of enzymes are described in the pathways thiosulfate disproportionation I (thiol-dependent), thiosulfate disproportionation II (non thiol-dependent) and thiosulfate disproportionation III (rhodanese), respectively.

About This Pathway

Thiosulfate sulfurtransferase is more often referred to by the name rhodanese, from the German word for thiocyanate, "rhodanid". The enzyme catalyzes the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. The original description of rhodanese, purified from bovine mitochondria, used thiosulfate and cyanide for this purpose. Rhodanese is a widespread enzyme, and has been detected in many major phyla, both prokaryotic and eukaryotic [Westley83]. Despite its ubiquity, the physiological role of rhodanese has not yet been established unambiguously. It has been suggested that rhodanese is involved in detoxification of cyanide in both mammals [Westley88, Nandi00] and bacteria [Cipollone08]. It has also been proposed that rhodanese, using the dithiol dihydrolipoate as the sulfur acceptor, may act as a sulfur insertase involved in the formation of prosthetic groups in iron-sulfur proteins, such as ferredoxin [Pagani84, Bonomi85].

Rhodanese performs the reaction by a double displacement formal mechanism. The crystal structure of rhodanese from Azotobacter vinelandii has been determined at 1.8 Å, and the study revealed that the active form of the enzyme is a persulfide, where a sulfur is attached to the active cysteine residue [Bordo00]. Unlike the enzyme thiosulfate—thiol sulfurtransferase, which catalyzes a similar reaction in which thiosulfate is disproportionated into sulfite and hydrogen sulfide, monothiols such as glutathione are poor substrates for rhodanese [Villarejo63, Volini66, Ray00].

The distinction between thiosulfate reductase and rhodanese is not always straight forward. For example, Aird et al purified an enzyme from Acinetobacter calcoaceticus that could catalyze either reaction under different conditions [Aird87].

Variants: superpathway of sulfur metabolism (Desulfocapsa sulfoexigens), thiosulfate disproportionation I (thiol-dependent), thiosulfate disproportionation II (non thiol-dependent)

Unification Links: EcoCyc:PWY-5350

Created 29-Sep-2006 by Caspi R, SRI International


Aird87: Aird BA, Heinrikson RL, Westley J (1987). "Isolation and characterization of a prokaryotic sulfurtransferase." J Biol Chem 262(36);17327-35. PMID: 3480285

Bonomi85: Bonomi F, Pagani S, Kurtz DM (1985). "Enzymic synthesis of the 4Fe-4S clusters of Clostridium pasteurianum ferredoxin." Eur J Biochem 148(1);67-73. PMID: 2983992

Bordo00: Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S, Bolognesi M (2000). "The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families." J Mol Biol 298(4);691-704. PMID: 10788330

Cipollone08: Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P (2008). "Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese." J Mol Microbiol Biotechnol 15(2-3);199-211. PMID: 18685272

Hashwa72: Hashwa F, Pfennig N (1972). "The reductive enzymatic cleavage of thiosulfate. Methods and appliction." Arch Mikrobiol 81(1);36-44. PMID: 4552952

Nandi00: Nandi DL, Horowitz PM, Westley J (2000). "Rhodanese as a thioredoxin oxidase." Int J Biochem Cell Biol 32(4);465-73. PMID: 10762072

Pagani84: Pagani S, Bonomi F, Cerletti P (1984). "Enzymic synthesis of the iron-sulfur cluster of spinach ferredoxin." Eur J Biochem 142(2);361-6. PMID: 6430704

Ray00: Ray WK, Zeng G, Potters MB, Mansuri AM, Larson TJ (2000). "Characterization of a 12-kilodalton rhodanese encoded by glpE of Escherichia coli and its interaction with thioredoxin." J Bacteriol 2000;182(8);2277-84. PMID: 10735872

Villarejo63: Villarejo M, Westley J (1963). "Mechanism of rhodanese catalysis of thiosulfate-lipoate oxidation-reduction." J Biol Chem 238;4016-20. PMID: 14086740

Volini66: Volini M, Westley J (1966). "The mechanism of the rhodanese-catalyzed thiosulfate-lipoate reaction. Kinetic analysis." J Biol Chem 241(22);5168-76. PMID: 5333153

Westley83: Westley J, Adler H, Westley L, Nishida C (1983). "The sulfurtransferases." Fundam Appl Toxicol 3(5);377-82. PMID: 6357923

Westley88: Westley J (1988). "Mammalian cyanide detoxification with sulphane sulphur." Ciba Found Symp 140;201-18. PMID: 3073057

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Adams02: Adams H, Teertstra W, Koster M, Tommassen J (2002). "PspE (phage-shock protein E) of Escherichia coli is a rhodanese." FEBS Lett 518(1-3);173-6. PMID: 11997041

Alexander87: Alexander K, Volini M (1987). "Properties of an Escherichia coli rhodanese." J Biol Chem 262(14);6595-604. PMID: 3553189

Belenky11: Belenky P, Collins JJ (2011). "Microbiology. Antioxidant strategies to tolerate antibiotics." Science 334(6058);915-6. PMID: 22096180

Bordo00a: Bordo D, Larson TJ, Donahue JL, Spallarossa A, Bolognesi M (2000). "Crystals of GlpE, a 12 kDa sulfurtransferase from escherichia coli, display 1.06 A resolution diffraction: a preliminary report." Acta Crystallogr D Biol Crystallogr 56(Pt 12);1691-3. PMID: 11092948

Bordo01: Bordo D, Forlani F, Spallarossa A, Colnaghi R, Carpen A, Bolognesi M, Pagani S (2001). "A persulfurated cysteine promotes active site reactivity in Azotobacter vinelandii Rhodanese." Biol Chem 382(8);1245-52. PMID: 11592406

BRENDA14: BRENDA team (2014). Imported from BRENDA version existing on Aug 2014.

Brissette91: Brissette JL, Weiner L, Ripmaster TL, Model P (1991). "Characterization and sequence of the Escherichia coli stress-induced psp operon." J Mol Biol 220(1);35-48. PMID: 1712397

Cereda09: Cereda A, Carpen A, Picariello G, Tedeschi G, Pagani S (2009). "The lack of rhodanese RhdA affects the sensitivity of Azotobacter vinelandii to oxidative events." Biochem J 418(1);135-43. PMID: 18925874

Charles66: Charles, A. M., Suzuki, I. (1966). "Mechanism of thiosulfate oxidation by Thiobacillus novellus." Biochim. Biophys. Acta 128: 510-521.

Cheng08: Cheng H, Donahue JL, Battle SE, Ray WK, Larson TJ (2008). "Biochemical and Genetic Characterization of PspE and GlpE, Two Single-domain Sulfurtransferases of Escherichia coli." Open Microbiol J 2;18-28. PMID: 19088907

Choi91: Choi YL, Kawase S, Kawamukai M, Sakai H, Komano T (1991). "Regulation of glpD and glpE gene expression by a cyclic AMP-cAMP receptor protein (cAMP-CRP) complex in Escherichia coli." Biochim Biophys Acta 1088(1);31-5. PMID: 1846566

Cipollone07: Cipollone R, Ascenzi P, Visca P (2007). "Common themes and variations in the rhodanese superfamily." IUBMB Life 59(2);51-9. PMID: 17454295

Colnaghi01: Colnaghi R, Cassinelli G, Drummond M, Forlani F, Pagani S (2001). "Properties of the Escherichia coli rhodanese-like protein SseA: contribution of the active-site residue Ser240 to sulfur donor recognition." FEBS Lett 500(3);153-6. PMID: 11445076

Colnaghi96: Colnaghi R, Pagani S, Kennedy C, Drummond M (1996). "Cloning, sequence analysis and overexpression of the rhodanese gene of Azotobacter vinelandii." Eur J Biochem 236(1);240-8. PMID: 8617271

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Eichmann14: Eichmann C, Tzitzilonis C, Bordignon E, Maslennikov I, Choe S, Riek R (2014). "Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli." J Biol Chem 289(34);23482-503. PMID: 24958726

Fukumori89: Fukumori Y, Hoshiko K, Yamanaka T (1989). "Purification and some properties of thiosulphate-cleaving enzyme from Thiobacillus novellus." FEMS Microbiol Lett 65:159-164. PMID: 2612884

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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