Thiosulfate—dithiol sulfurtransferase

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thiosulfate-dithiol sulfurtransferase
Identifiers
EC no. 2.8.1.5
CAS no. 9059-49-8
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In enzymology, a thiosulfate-dithiol sulfurtransferase (EC 2.8.1.5) is an enzyme that catalyzes the chemical reaction

thiosulfate + dithioerythritol sulfite + 4,5-cis-dihydroxy-1,2-dithiacyclohexane (i.e. oxidized dithioerythritol) + sulfide

Thus, the two substrates of this enzyme are thiosulfate and dithioerythritol, whereas its 3 products are sulfite, 4,5-cis-dihydroxy-1,2-dithiacyclohexane, and sulfide.

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is thiosulfate:dithioerythritol sulfurtransferase. Other names in common use include thiosulfate reductase, and TSR. This enzyme participates in sulfur metabolism.

Related Research Articles

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Sulfate-reducing microorganisms (SRM) or sulfate-reducing prokaryotes (SRP) are a group composed of sulfate-reducing bacteria (SRB) and sulfate-reducing archaea (SRA), both of which can perform anaerobic respiration utilizing sulfate (SO2−
4
) as terminal electron acceptor, reducing it to hydrogen sulfide (H2S). Therefore, these sulfidogenic microorganisms "breathe" sulfate rather than molecular oxygen (O2), which is the terminal electron acceptor reduced to water (H2O) in aerobic respiration.

<span class="mw-page-title-main">Metal dithiolene complex</span>

Dithiolene metal complexes are complexes containing 1,2-dithiolene ligands. 1,2-Dithiolene ligands, a particular case of 1,2-dichalcogenolene species along with 1,2-diselenolene derivatives, are unsaturated bidentate ligand wherein the two donor atoms are sulfur. 1,2-Dithiolene metal complexes are often referred to as "metal dithiolenes", "metallodithiolenes" or "dithiolene complexes". Most molybdenum- and tungsten-containing proteins have dithiolene-like moieties at their active sites, which feature the so-called molybdopterin cofactor bound to the Mo or W.

<span class="mw-page-title-main">Thiosulfate</span> Polyatomic ion (S2O3, charge –2)

Thiosulfate is an oxyanion of sulfur with the chemical formula S2O2−3. Thiosulfate also refers to the compounds containing this anion, which are the salts of thiosulfuric acid, e.g. sodium thiosulfate Na2S2O3. Thiosulfate also refers to the esters of thiosulfuric acid. The prefix thio- indicates that the thiosulfate is a sulfate with one oxygen replaced by sulfur. Thiosulfate is tetrahedral at the central S atom. Thiosulfate salts occur naturally. Thiosulfate ion has C3v symmetry, and is produced by certain biochemical processes. It rapidly dechlorinates water and is notable for its use to halt bleaching in the paper-making industry. Thiosulfate salts are mainly used in dying in textiles and the bleaching of natural substances.

<span class="mw-page-title-main">Sulfur assimilation</span> Incorporation of sulfur into living organisms

Sulfur assimilation is the process by which living organisms incorporate sulfur into their biological molecules. In plants, sulfate is absorbed by the roots and then be transported to the chloroplasts by the transipration stream where the sulfur are reduced to sulfide with the help of a series of enzymatic reactions. Furthermore, the reduced sulfur is incorporated into cysteine, an amino acid that is a precursor to many other sulfur-containing compounds. In animals, sulfur assimilation occurs primarily through the diet, as animals cannot produce sulfur-containing compounds directly. Sulfur is incorporated into amino acids such as cysteine and methionine, which are used to build proteins and other important molecules. Besides, With the rapid development of economy, the increase emission of sulfur results in environmental issues, such as acid rain and hydrogen sulfilde.

<span class="mw-page-title-main">Rhodanese</span> Mitochondrial enzyme which breaks down cyanide

Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN) by converting it to thiocyanate. In enzymatology, the common name is listed as thiosulfate sulfurtransferase. The diagram on the right shows the crystallographically-determined structure of rhodanese.

In enzymology, a phthalate 4,5-cis-dihydrodiol dehydrogenase (EC 1.3.1.64) is an enzyme that catalyzes the chemical reaction

In enzymology, a phthalate 4,5-dioxygenase (EC 1.14.12.7) is an enzyme that catalyzes the chemical reaction

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In enzymology, a sulfur oxygenase/reductase (EC 1.13.11.55) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Adenylyl-sulfate reductase</span> Class of enzymes

Adenylyl-sulfate reductase is an enzyme that catalyzes the chemical reaction of the reduction of adenylyl-sulfate/adenosine-5'-phosphosulfate (APS) to sulfite through the use of an electron donor cofactor. The products of the reaction are AMP and sulfite, as well as an oxidized electron donor cofactor.

<span class="mw-page-title-main">Sulfite reductase</span> Enzyme family

Sulfite reductases (EC 1.8.99.1) are enzymes that participate in sulfur metabolism. They catalyze the reduction of sulfite to hydrogen sulfide and water. Electrons for the reaction are provided by a dissociable molecule of either NADPH, bound flavins, or ferredoxins.

<span class="mw-page-title-main">Thiosulfate dehydrogenase</span>

Thiosulfate dehydrogenase is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">3-mercaptopyruvate sulfurtransferase</span> Class of enzymes

In enzymology, a 3-mercaptopyruvate sulfurtransferase is an enzyme that catalyzes the chemical reactions of 3-mercaptopyruvate. This enzyme belongs to the family of transferases, specifically the sulfurtransferases. This enzyme participates in cysteine metabolism. It is encoded by the MPST gene.

In enzymology, a thiosulfate-thiol sulfurtransferase is an enzyme that catalyzes the chemical reaction

Sulfur is metabolized by all organisms, from bacteria and archaea to plants and animals. Sulfur can have an oxidation state from -2 to +6 and is reduced or oxidized by a diverse range of organisms. The element is present in proteins, sulfate esters of polysaccharides, steroids, phenols, and sulfur-containing coenzymes.

<span class="mw-page-title-main">Siroheme</span>

Siroheme is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. It is a cofactor at the active site of sulfite reductase, which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide, which can be incorporated into the organic compound homocysteine.

<span class="mw-page-title-main">Dissimilatory sulfate reduction</span>

Dissimilatory sulfate reduction is a form of anaerobic respiration that uses sulfate as the terminal electron acceptor to produce hydrogen sulfide. This metabolism is found in some types of bacteria and archaea which are often termed sulfate-reducing organisms. The term "dissimilatory" is used when hydrogen sulfide is produced in an anaerobic respiration process. By contrast, the term "assimilatory" would be used in relation to the biosynthesis of organosulfur compounds, even though hydrogen sulfide may be an intermediate.

<span class="mw-page-title-main">Sulfoxylic acid</span> Chemical compound

Sulfoxylic acid (H2SO2) (also known as hyposulfurous acid or sulfur dihydroxide) is an unstable oxoacid of sulfur in an intermediate oxidation state between hydrogen sulfide and dithionous acid. It consists of two hydroxy groups attached to a sulfur atom. Sulfoxylic acid contains sulfur in an oxidation state of +2. Sulfur monoxide (SO) can be considered as a theoretical anhydride for sulfoxylic acid, but it is not actually known to react with water.

<span class="mw-page-title-main">Microbial oxidation of sulfur</span>

Microbial oxidation of sulfur is the oxidation of sulfur by microorganisms to build their structural components. The oxidation of inorganic compounds is the strategy primarily used by chemolithotrophic microorganisms to obtain energy to survive, grow and reproduce. Some inorganic forms of reduced sulfur, mainly sulfide (H2S/HS) and elemental sulfur (S0), can be oxidized by chemolithotrophic sulfur-oxidizing prokaryotes, usually coupled to the reduction of oxygen (O2) or nitrate (NO3). Anaerobic sulfur oxidizers include photolithoautotrophs that obtain their energy from sunlight, hydrogen from sulfide, and carbon from carbon dioxide (CO2).

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References