Carbonyl sulfide hydrolase

Last updated
Carbonyl sulfide hydrolase (COSase)
Identifiers
EC no. 3.13.1.7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
Search
PMC articles
PubMed articles
NCBI proteins
Carbonyl Sulfide Hydrolase (COSase)
Identifiers
SymbolCarbonyl Sulfide Hydrolase (COSase)
Pfam PF00484
InterPro IPR036874 IPR001765, IPR036874
SMART SM00947
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Carbonyl sulfide hydrolase (EC 3.13.1.7; abbreviated as COSase) is an enzyme that degrades carbonyl sulfide (COS) to hydrogen sulfide (H2S) and carbon dioxide (CO2). Isolated from Thiobacillus thioparus bacterium, the potential of COSase would reduce the high global warming effect of COS and change the ozone chemistry, because COS is the source of sulfur in the troposphere. [1] [2] [3]

Contents

Etymology

Being that it is a hydrolase, which is an enzyme that uses water to break chemical bonds, the name suggests that within the mechanism are water molecules that are involved in disseminating molecules within the reaction. The very name when broken down means that it is an enzyme that breaks down carbonyl sulfide.

History

COSase was isolated, characterized and structure was determined from Thiobacillus thioparus bacterium. In search for a chemical method to break down COS more efficiently than the biologically established methods that employ the soil environment for degradation enzymes. These enzymes are carbonic anhydrase, carbonic disulfide hydrolase, nitrogenase, carbon monoxide, and RuBisCO. [4] [5] [6] [7] [8] [9] [10] [11] [12] The enzymes listed are limited in their use due to specificities and optimal environments, which is why chemical development of an enzyme unique to catalyzing the degradation of COS is researched. - Thiobacillus thioparus is a bacterium found both in soil and freshwater and is known for its sulfur-oxidizing properties. The strain used to create COSase is THI11, which was originally isolated as a thiocyanate degrading microorganism. [13] The enzyme was found by putting the extract of T. thioparus strain THI115 through column chromatography to purify it and ICP-MS to deduce the structure. [1]

Structure

Using sodium dodecyl sulfate–polyacrylamide gel electrophoresis, a subunit molecular mass of 27 kDa was found. [1] After testing for expression in E. coli the true molecular mass of ~94 kDa was found by SEC-MALS. [1] ICP-MS shows that there is one zinc ion per sub unit. [1] 35 amino acid sequence found on the N-terminal: MEKSNTDALLENNRLYAGGQATHRPGHPGMQPIQP. [1] There are five strands (β1−β5) that make up β-sheet core and four α-helices (α1, α2, α3, and α6) in its flank, with two additional helices (α4 and α5) that protrude from its core. They arrange in homodimer pairs to form ten-stranded β-sheets. [1] Between two subunits of a homodimer is the catalytic site. Cys44, His97, Cys 100, and a water molecule coordinate with a zinc ion, with a thiocyanate molecule in the catalytic site pocket. [1]

Function

COSase is responsible for the degradation of COS to H2S and CO2 in the second step of SCN assimilation. It hydrolyzes COS with a certain specificity over a wide range of concentrations both in vivo and in vitro. [1]

Mechanism

Thiocyanate hydrolase (SCNase) found in THI115 initiates enzymatic formation of thiocyanate (SCN). SCNase hydrolyzes SCN to ammonia and COS. The COS that results from the hydrolysis is metabolized to form hydrogen sulfide (H2S) which is oxidized to sulfate to produce energy. [14] [15] [16] [17] [18]

Hydroxide and zinc io ns perform a nucleophilic attack on the carbon in the COS molecule, which creates an intermediate with zinc bound to hydroxide oxygen and sulfur of the COS molecule. Oxygen is then released from zinc and forms CO2. Water from the solvent interacts with the su lfur-zinc ion and regenerates the active site and releases H2S. [1]

Carbonyl sulfide hydrolase inhibitor

COSase is weakly inhibited by SCN. [1]

Related Research Articles

<span class="mw-page-title-main">Sulfur</span> Chemical element, symbol S and atomic number 16

Sulfur (also spelled sulphur in British English) is a chemical element with the symbol S and atomic number 16. It is abundant, multivalent and nonmetallic. Under normal conditions, sulfur atoms form cyclic octatomic molecules with a chemical formula S8. Elemental sulfur is a bright yellow, crystalline solid at room temperature.

<span class="mw-page-title-main">Metalloprotein</span> Protein that contains a metal ion cofactor

Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.

<span class="mw-page-title-main">Carbon disulfide</span> Neurotoxic compound with formula S=C=S

Carbon disulfide is an inorganic compound with the chemical formula CS2 and structure S=C=S. It is a colorless, flammable, neurotoxic liquid that is used as a building block in organic synthesis. Pure carbon disulfide has a pleasant, ether- or chloroform-like odor, but commercial samples are usually yellowish and are typically contaminated with foul-smelling impurities.

Sulfide (British English also sulphide) is an inorganic anion of sulfur with the chemical formula S2− or a compound containing one or more S2− ions. Solutions of sulfide salts are corrosive. Sulfide also refers to chemical compounds large families of inorganic and organic compounds, e.g. lead sulfide and dimethyl sulfide. Hydrogen sulfide (H2S) and bisulfide (SH) are the conjugate acids of sulfide.

The iron–sulfur world hypothesis is a set of proposals for the origin of life and the early evolution of life advanced in a series of articles between 1988 and 1992 by Günter Wächtershäuser, a Munich patent lawyer with a degree in chemistry, who had been encouraged and supported by philosopher Karl R. Popper to publish his ideas. The hypothesis proposes that early life may have formed on the surface of iron sulfide minerals, hence the name. It was developed by retrodiction from extant biochemistry in conjunction with chemical experiments.

Hydrolase is a class of enzymes that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.

In chemistry, disproportionation, sometimes called dismutation, is a redox reaction in which one compound of intermediate oxidation state converts to two compounds, one of higher and one of lower oxidation states. The reverse of disproportionation, such as when a compound in an intermediate oxidation state is formed from precursors of lower and higher oxidation states, is called comproportionation, also known as synproportionation.

Amine gas treating, also known as amine scrubbing, gas sweetening and acid gas removal, refers to a group of processes that use aqueous solutions of various alkylamines (commonly referred to simply as amines) to remove hydrogen sulfide (H2S) and carbon dioxide (CO2) from gases. It is a common unit process used in refineries, and is also used in petrochemical plants, natural gas processing plants and other industries.

<span class="mw-page-title-main">Carbonyl sulfide</span> Chemical compound

Carbonyl sulfide is the chemical compound with the linear formula OCS. It is a colorless flammable gas with an unpleasant odor. It is a linear molecule consisting of a carbonyl

<span class="mw-page-title-main">Sulfur cycle</span> Biogeochemical cycle of sulfur

The sulfur cycle is a biogeochemical cycle in which the sulfur moves between rocks, waterways and living systems. It is important in geology as it affects many minerals and in life because sulfur is an essential element (CHNOPS), being a constituent of many proteins and cofactors, and sulfur compounds can be used as oxidants or reductants in microbial respiration. The global sulfur cycle involves the transformations of sulfur species through different oxidation states, which play an important role in both geological and biological processes. Steps of the sulfur cycle are:

<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 thiocyanate hydrolase (EC 3.5.5.8) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Carl von Than</span> Hungarian chemist (1834–1908)

Károly Antal Than de Apát – also called as Carl von Than – was a Hungarian chemist who discovered carbonyl sulfide in 1867.

Zinc compounds are chemical compounds containing the element zinc which is a member of the group 12 of the periodic table. The oxidation state of zinc in most compounds is the group oxidation state of +2. Zinc may be classified as a post-transition main group element with zinc(II). Zinc compounds are noteworthy for their nondescript behavior, they are generally colorless, do not readily engage in redox reactions, and generally adopt symmetrical structures.

Sulfanyl (HS), also known as the mercapto radical, hydrosulfide radical, or hydridosulfur, is a simple radical molecule consisting of one hydrogen and one sulfur atom. The radical appears in metabolism in organisms as H2S is detoxified. Sulfanyl is one of the top three sulfur-containing gasses in gas giants such as Jupiter and is very likely to be found in brown dwarfs and cool stars. It was originally discovered by Margaret N. Lewis and John U. White at the University of California in 1939. They observed molecular absorption bands around 325 nm belonging to the system designated by 2Σ+2Πi. They generated the radical by means of a radio frequency discharge in hydrogen sulfide. HS is formed during the degradation of hydrogen sulfide in the atmosphere of the Earth. This may be a deliberate action to destroy odours or a natural phenomenon.

<span class="mw-page-title-main">Disulfur dioxide</span> Chemical compound

Disulfur dioxide, dimeric sulfur monoxide or SO dimer is an oxide of sulfur with the formula S2O2. The solid is unstable with a lifetime of a few seconds at room temperature.

<span class="mw-page-title-main">Carbonic anhydrase</span> Class of enzymes

The carbonic anhydrases form a family of enzymes that catalyze the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid. The active site of most carbonic anhydrases contains a zinc ion. They are therefore classified as metalloenzymes. The enzyme maintains acid-base balance and helps transport carbon dioxide.

A heterocumulene is a molecule or ion containing a chain of at least three double bonds between consecutive atoms, in which one or more atoms in the doubly bonded chain is a heteroatom. Such species are analogous to a cumulene in which the chain of doubly bonded atoms contains only carbon, except that at least one carbon is replaced by a heteroatom. Some authors relax the definition to include species with chains of only two double bonds between consecutive atoms, also known as heteroallenes.

Carbon disulfide hydrolase is an enzyme with a molecular mass of 23,576 Da. The enzyme is hexadecameric. It catalyzes the hydrolysis of carbon disulfide.

<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.

References

  1. 1 2 3 4 5 6 7 8 9 10 11 Ogawa T, Noguchi K, Saito M, Nagahata Y, Kato H, Ohtaki A, et al. (March 2013). "Carbonyl sulfide hydrolase from Thiobacillus thioparus strain THI115 is one of the β-carbonic anhydrase family enzymes". Journal of the American Chemical Society. 135 (10): 3818–25. doi:10.1021/ja307735e. PMID   23406161.
  2. Chin M, Davis DD (1995). "A reanalysis of carbonyl sulfide as a source of stratospheric background sulfur aerosol". Journal of Geophysical Research. 100 (D5): 8993. Bibcode:1995JGR...100.8993C. doi:10.1029/95JD00275.
  3. Andreae MO (16 May 1997). "Atmospheric Aerosols: Biogeochemical Sources and Role in Atmospheric Chemistry". Science. 276 (5315): 1052–1058. doi:10.1126/science.276.5315.1052.
  4. Supuran CT (February 2008). "Carbonic anhydrases: novel therapeutic applications for inhibitors and activators". Nature Reviews. Drug Discovery. 7 (2): 168–81. doi:10.1038/nrd2467. PMID   18167490. S2CID   3833178.
  5. Seefeldt LC, Rasche ME, Ensign SA (April 1995). "Carbonyl sulfide and carbon dioxide as new substrates, and carbon disulfide as a new inhibitor, of nitrogenase". Biochemistry. 34 (16): 5382–9. doi:10.1021/bi00016a009. PMID   7727396.
  6. Protoschill-Krebs G, Wilhelm C, Kesselmeier J (September 1996). "Consumption of carbonyl sulphide (COS) by higher plant carbonic anhydrase (CA)". Atmospheric Environment. 30 (18): 3151–3156. Bibcode:1996AtmEn..30.3151P. doi:10.1016/1352-2310(96)00026-X.
  7. Miller AG, Espie GS, Canvin DT (July 1989). "Use of Carbon Oxysulfide, a Structural Analog of CO(2), to Study Active CO(2) Transport in the Cyanobacterium Synechococcus UTEX 625". Plant Physiology. 90 (3): 1221–31. doi:10.1104/pp.90.3.1221. PMC   1061868 . PMID   16666875.
  8. Lorimer GH, Pierce J (February 1989). "Carbonyl sulfide: an alternate substrate for but not an activator of ribulose-1,5-bisphosphate carboxylase". The Journal of Biological Chemistry. 264 (5): 2764–72. doi: 10.1016/S0021-9258(19)81679-4 . PMID   2492523.
  9. Haritos VS, Dojchinov G (January 2005). "Carbonic anhydrase metabolism is a key factor in the toxicity of CO2 and COS but not CS2 toward the flour beetle Tribolium castaneum [Coleoptera: Tenebrionidae]". Comparative Biochemistry and Physiology. Toxicology & Pharmacology. 140 (1): 139–47. doi:10.1016/j.cca.2005.01.012. PMID   15792633.
  10. Ensign SA (April 1995). "Reactivity of carbon monoxide dehydrogenase from Rhodospirillum rubrum with carbon dioxide, carbonyl sulfide, and carbon disulfide". Biochemistry. 34 (16): 5372–8. doi:10.1021/bi00016a008. PMID   7727395.
  11. Chengelis CP, Neal RA (October 1979). "Hepatic carbonyl sulfide metabolism". Biochemical and Biophysical Research Communications. 90 (3): 993–9. doi:10.1016/0006-291X(79)91925-9. PMID   116662.
  12. Alterio V, Di Fiore A, D'Ambrosio K, Supuran CT, De Simone G (August 2012). "Multiple binding modes of inhibitors to carbonic anhydrases: how to design specific drugs targeting 15 different isoforms?". Chemical Reviews. 112 (8): 4421–68. doi:10.1021/cr200176r. hdl: 2158/776392 . PMID   22607219.
  13. Katayama Y, Narahara Y, Inoue Y, Amano F, Kanagawa T, Kuraishi H (May 1992). "A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme catalyzing the formation of carbonyl sulfide from thiocyanate". The Journal of Biological Chemistry. 267 (13): 9170–5. doi: 10.1016/S0021-9258(19)50404-5 . PMID   1577754.
  14. Sauze J, Ogée J, Maron PA, Crouzet O, Nowak V, Wohl S, et al. (December 2017). "18O and OCS exchange". Soil Biology & Biochemistry. 115: 371–382. doi:10.1016/j.soilbio.2017.09.009. PMC   5666291 . PMID   29200510.
  15. Berben T, Balkema C, Sorokin DY, Muyzer G (26 December 2017). "T Using Transcriptomics". mSystems. 2 (6): mSystems.00102–17, e00102–17. doi:10.1128/mSystems.00102-17. PMC   5744179 . PMID   29285524.
  16. Sun W, Kooijmans LM, Maseyk K, Chen H, Mammarella I, Vesala T, Levula J, Keskinen H, Seibt U (1 February 2018). "Soil fluxes of carbonyl sulfide (COS), carbon monoxide, and carbon dioxide in a boreal forest in southern Finland". Atmospheric Chemistry and Physics. 18 (2): 1363–1378. Bibcode:2018ACP....18.1363S. doi: 10.5194/acp-18-1363-2018 .
  17. Sun W, Maseyk K, Lett C, Seibt U (4 June 2018). "Stomatal control of leaf fluxes of carbonyl sulfide and CO<sub>2</sub> in a <i>Typha</i> freshwater marsh". Biogeosciences. 15 (11): 3277–3291. Bibcode:2018BGeo...15.3277S. doi: 10.5194/bg-15-3277-2018 .
  18. Zhao S, Yi H, Tang X, Kang D, Yu Q, Gao F, Wang J, Huang Y, Yang Z (1 February 2018). "Mechanism of activity enhancement of the Ni based hydrotalcite-derived materials in carbonyl sulfide removal". Materials Chemistry and Physics. 205: 35–43. doi:10.1016/j.matchemphys.2017.11.002.

Further reading