Coenzyme-B sulfoethylthiotransferase

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coenzyme-B sulfoethylthiotransferase
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EC no. 2.8.4.1
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In enzymology, coenzyme-B sulfoethylthiotransferase, also known as methyl-coenzyme M reductase (MCR) or most systematically as 2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreonine S-(2-sulfoethyl)thiotransferase is an enzyme that catalyzes the final step in the formation of methane. [1] It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. Via this enzyme, most of the natural gas on earth was produced. Ruminants (e.g. cows) produce methane because their rumens contain methanogenic prokaryotes (Archaea) [2] [3] that encode and express the set of genes of this enzymatic complex.

Contents

The enzyme has two active sites, each occupied by the nickel-containing F430 cofactor. [4]

methyl-CoM2-(methylthio)ethanesulfonate + coenzyme BN-(7-mercaptoheptanoyl)threonine 3-O-phosphate CoM-S-S-CoB + methane
Structure of 2-mercaptoethanesulfonate (coenzyme M: reacts after methylation on the thiol) Coenzyme M (CoM).svg
Structure of 2-mercaptoethanesulfonate (coenzyme M: reacts after methylation on the thiol)
Structure of N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Coenzyme B (CoB).svg
Structure of N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)

The two substrates of this enzyme are 2-(methylthio)ethanesulfonate and N-(7-mercaptoheptanoyl)threonine 3-O-phosphate; its two products are CoM-S-S-CoB and methane. 3-Nitrooxypropanol inhibits the enzyme. [5]

In some species, the enzyme reacts in reverse (a process called reverse methanogenesis ), catalysing the anaerobic oxidation of methane, therefore removing it from the environment. [6] Such organisms are methanotrophs.

This enzyme belongs to the family of transferases, specifically those transferring alkylthio groups.

This enzyme participates in folate biosynthesis.[ citation needed ]

Structure

Coenzyme-B sulfoethylthiotransferase is a multiprotein complex made up of a pair of identical halves. Each half is made up of three subunits: α, β and γ, [7] also called McrA, McrB and McrG, respectively.

Related Research Articles

<span class="mw-page-title-main">Cofactor (biochemistry)</span> Non-protein chemical compound or metallic ion

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst. Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound.

Methanogens are microorganisms that produce methane as a metabolic byproduct in hypoxic conditions. They belong to the domain Archaea and are members of the phylum Euryarchaeota. Methanogens are common in wetlands, where they are responsible for marsh gas, and can occur in the digestive tracts of animals including ruminants and humans, where they are responsible for the methane content of belching and flatulence. In marine sediments, the biological production of methane, termed methanogenesis, is generally confined to where sulfates are depleted below the top layers and methanogens play an indispensable role in anaerobic wastewater treatments. Other methanogens are extremophiles, found in environments such as hot springs and submarine hydrothermal vents as well as in the "solid" rock of Earth's crust, kilometers below the surface.

Methanogenesis or biomethanation is the formation of methane coupled to energy conservation by microbes known as methanogens. Organisms capable of producing methane for energy conservation have been identified only from the domain Archaea, a group phylogenetically distinct from both eukaryotes and bacteria, although many live in close association with anaerobic bacteria. The production of methane is an important and widespread form of microbial metabolism. In anoxic environments, it is the final step in the decomposition of biomass. Methanogenesis is responsible for significant amounts of natural gas accumulations, the remainder being thermogenic.

Tetrahydromethanopterin is a coenzyme in methanogenesis. It is the carrier of the C1 group as it is reduced to the methyl level, before transferring to the coenzyme M.

<span class="mw-page-title-main">Coenzyme M</span> Chemical compound

Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaeal methanogens, and in the metabolism of other substrates in bacteria. It is also a necessary cofactor in the metabolic pathway of alkene-oxidizing bacteria. CoM helps eliminate the toxic epoxides formed from the oxidation of alkenes such as propylene. The structure of this coenzyme was discovered by CD Taylor and RS Wolfe in 1974 while they were studying methanogenesis, the process by which carbon dioxide is transformed into methane in some anaerobic bacteria. The coenzyme is an anion with the formula HSCH
2
CH
2
SO
3
. It is named 2-mercaptoethanesulfonate and abbreviated HS–CoM. The cation is unimportant, but the sodium salt is most available. Mercaptoethanesulfonate contains both a thiol, which is the main site of reactivity, and a sulfonate group, which confers solubility in aqueous media.

Coenzyme B is a coenzyme required for redox reactions in methanogens. The full chemical name of coenzyme B is 7-mercaptoheptanoylthreoninephosphate. The molecule contains a thiol, which is its principal site of reaction.

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

Methanofurans are a family of chemical compounds found in methanogenic archaea. These species feature a 2-aminomethylfuran linked to phenoxy group. At least three different end groups are recognized: R = tricarboxyheptanoyl (methanofuran), glutamyl-glutamyl, tricarboxy-2-hydroxyheptanoyl.

In enzymology, a tetrahydromethanopterin S-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) (EC 1.2.7.7) is an enzyme that catalyzes the chemical reaction

In enzymology, a 5,10-methylenetetrahydromethanopterin reductase (EC 1.5.98.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a CoB—CoM heterodisulfide reductase (EC 1.8.98.1) is an enzyme that catalyzes the chemical reaction

Coenzyme F<sub>420</sub> Chemical compound

Coenzyme F420 is a family of coenzymes involved in redox reactions in a number of bacteria and archaea. It is derived from coenzyme FO (7,8-didemethyl-8-hydroxy-5-deazariboflavin) and differs by having a oligoglutamyl tail attached via a 2-phospho-L-lactate bridge. F420 is so named because it is a flavin derivative with an absorption maximum at 420 nm.

<span class="mw-page-title-main">Cofactor F430</span> Chemical compound

F430 is the cofactor (sometimes called the coenzyme) of the enzyme methyl coenzyme M reductase (MCR). MCR catalyzes the reaction EC 2.8.4.1 that releases methane in the final step of methanogenesis:

(Methyl-Co methanol-specific corrinoid protein):coenzyme M methyltransferase is an enzyme with systematic name methylated methanol-specific corrinoid protein:coenzyme M methyltransferase. This enzyme catalyses the following chemical reaction

Tetramethylammonium-corrinoid protein Co-methyltransferase is an enzyme with systematic name tetramethylammonium:5-hydroxybenzimidazolylcobamide Co-methyltransferase. This enzyme catalyses the following chemical reaction

Methanococcus maripaludis is a species of methanogenic archaea found in marine environments, predominantly salt marshes. M. maripaludis is a weakly motile, non-spore-forming, Gram-negative, strict anaerobic mesophile with a pleomorphic coccoid-rod shape, averaging 1.2 by 1.6 μm is size. The genome of M. maripaludis has been sequenced, and over 1,700 protein-coding genes have been identified. In ideal conditions, M. maripaludis grows quickly and can double every two hours.

<span class="mw-page-title-main">3-Nitrooxypropanol</span> Chemical compound

3-Nitrooxypropanol, abbreviated 3NOP, is an organic compound with the formula HOCH2CH2CH2ONO2. It is the mononitrate ester of 1,3-propanediol. The compound is an inhibitor of the enzyme methyl coenzyme M reductase (MCR). MCR catalyzes the final step in methanogenesis. When it is fed to ruminants, their methane production is diminished. In 2021 Bovaer, a feed additive for cows produced by DSM based on this compound, has been approved in Brazil, one of the world's largest meat exporters and also Chile. In 2022, it was approved for use on dairy cows in the EU.

<span class="mw-page-title-main">C1 chemistry</span> One-carbon molecule chemical processes

C1 chemistry is the chemistry of one-carbon molecules. Although many compounds and ions contain only one carbon, stable and abundant C-1 feedstocks are the focus of research. Four compounds are of major industrial importance: methane, carbon monoxide, carbon dioxide, and methanol. Technologies that interconvert these species are often used massively to match supply to demand.

In enzymology, a formylmethanofuran dehydrogenase (EC 1.2.99.5) is an enzyme that catalyzes the chemical reaction:

Ralph Stoner Wolfe was an American microbiologist, who contributed to the discovery of the single-celled archaea as the third domain of life. He was a pioneer in the biochemistry of methanogenesis.

References

  1. Stephen W., Ragdale (2014). "Chapter 6. Biochemistry of Methyl-Coenzyme M Reductase: The Nickel Metalloenzyme that Catalyzes the Final Step in Synthesis and the First Step in Anaerobic Oxidation of the Greenhouse Gas Methane". In Peter M.H. Kroneck and Martha E. Sosa Torres (ed.). The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment. Metal Ions in Life Sciences. Vol. 14. Springer. pp. 125–145. doi:10.1007/978-94-017-9269-1_6. PMID   25416393.
  2. "Bovine Rumen - microbewiki".
  3. Whitford MF, Teather RM, Forster RJ (2001). "Phylogenetic analysis of methanogens from the bovine rumen". BMC Microbiology. 1: 5. doi: 10.1186/1471-2180-1-5 . PMC   32158 . PMID   11384509.
  4. Thauer RK (September 1998). "Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture". Microbiology. 144 (9): 2377–406. doi: 10.1099/00221287-144-9-2377 . PMID   9782487.
  5. Hristov AN, Oh J, Giallongo F, Frederick TW, Harper MT, Weeks HL, Branco AF, Moate PJ, Deighton MH, Williams SR, Kindermann M, Duval S (August 2015). "An inhibitor persistently decreased enteric methane emission from dairy cows with no negative effect on milk production". Proceedings of the National Academy of Sciences of the United States of America. 112 (34): 10663–8. Bibcode:2015PNAS..11210663H. doi: 10.1073/pnas.1504124112 . PMC   4553761 . PMID   26229078.
  6. Hallam SJ, Putnam N, Preston CM, Detter JC, Rokhsar D, Richardson PM, DeLong EF (September 2004). "Reverse methanogenesis: testing the hypothesis with environmental genomics". Science. 305 (5689): 1457–62. Bibcode:2004Sci...305.1457H. doi:10.1126/science.1100025. PMID   15353801. S2CID   31107045.
  7. Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK (November 1997). "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation". Science. 278 (5342): 1457–62. Bibcode:1997Sci...278.1457E. doi:10.1126/science.278.5342.1457. PMID   9367957.

Further reading