Methanofuran

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Structure of the methanofurans Methanofuran a b c.svg
Structure of the methanofurans

Methanofurans (MFRs) are a family of chemical compounds found in methanogenic archaea. [1] These species feature a 2-aminomethylfuran linked to phenoxy group. At least three different end groups are recognized: R = tricarboxyheptanoyl (methanofuran), glutamyl-glutamyl (methanofuran b), tricarboxy-2-hydroxyheptanoyl (methanofuran c, see picture).

Contents

Formylation of MFR

Methanofuran converts to formylmethanofuran in an early stage of methanogenesis. The enzyme formylmethanofuran dehydrogenase (EC: 1.2.99.5) formylates methanofuran using CO
2
, the primary C1 source in methanogenesis. [2]

Deformylation of MFR

The enzyme formylmethanofuran:tetrahydromethanopterin formyltransferase catalyzes the transfer of the formyl group from formylmethanofuran to N5 on tetrahydromethanopterin, H
4
MPT
. This enzyme has been crystallized; it contains no prosthetic group. [3]

Related Research Articles

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.

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

Pterin is a heterocyclic compound composed of a pteridine ring system, with a "keto group" and an amino group on positions 4 and 2 respectively. It is structurally related to the parent bicyclic heterocycle called pteridine. Pterins, as a group, are compounds related to pterin with additional substituents. Pterin itself is of no biological significance.

Methanopyrus is a genus of methanogen, with a single described species, Methanopyrus kandleri. It is a rod-shaped hyperthermophile, discovered on the wall of a black smoker from the Gulf of California at a depth of 2,000 m, at temperatures of 84–110 °C. Strain 116 was discovered in black smoker fluid of the Kairei hydrothermal field; it can survive and reproduce at 122 °C. M. kandleri also requires a high ionic concentration in order for growth and cellular activity. Due to the species' high resilience and extreme environment, M. kandleri is also classified as an extremophile. It lives in a hydrogen-carbon dioxide rich environment, and like other methanogens reduces the latter to methane. It is placed among the Euryarchaeota, in its own class.

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">Wood–Ljungdahl pathway</span> A set of biochemical reactions used by some bacteria

The Wood–Ljungdahl pathway is a set of biochemical reactions used by some bacteria. It is also known as the reductive acetyl-coenzyme A (Acetyl-CoA) pathway. This pathway enables these organisms to use hydrogen as an electron donor, and carbon dioxide as an electron acceptor and as a building block for biosynthesis.

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

<span class="mw-page-title-main">5,10-Methenyltetrahydromethanopterin hydrogenase</span> Class of enzymes

The 5,10-methenyltetrahydromethanopterin hydrogenase, the so-called iron-sulfur cluster-free hydrogenase, is an enzyme found in methanogenic archea such as Methanothermobacter marburgensis. It was discovered and first characterized by the Thauer group at the Max Planck Institute in Marburg. Hydrogenases are enzymes that either reduce protons or oxidize molecular dihydrogen.

<span class="mw-page-title-main">Coenzyme-B sulfoethylthiotransferase</span> Class of enzymes

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. 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 produce methane because their rumens contain methanogenic prokaryotes (Archaea) that encode and express the set of genes of this enzymatic complex.

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">Formylmethanofuran—tetrahydromethanopterin N-formyltransferase</span>

In enzymology, a formylmethanofuran-tetrahydromethanopterin N-formyltransferase is an enzyme that catalyzes the chemical reaction

Fermentative hydrogen production is the fermentative conversion of organic substrates to H2. Hydrogen produced in this manner is often called biohydrogen. The conversion is effected by bacteria and protozoa, which employ enzymes. Fermentative hydrogen production is one of several anaerobic conversions.

<span class="mw-page-title-main">Aerobic methane production</span> Potential biological pathway for atmospheric methane production

Aerobic methane production is a potential biological pathway for atmospheric methane (CH4) production under oxygenated conditions. The existence of this pathway was first theorized in 2006. While significant evidence suggests the existence of this pathway, it remains poorly understood and its existence is controversial. Naturally occurring methane is mainly produced by the process of methanogenesis, a form of anaerobic respiration used by microorganisms as an energy source. Methanogenesis usually only occurs under anoxic conditions. By contrast, aerobic methane production is thought to occur in oxygenated environments under near-ambient conditions. The process involves non-microbial methane generation from terrestrial plant-matter. Temperature and ultraviolet light are thought to be key factors in this process. Methane may also be produced under aerobic conditions in near-surface ocean water, a process which likely involves the degradation of methylphosphonate.

<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:

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">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:

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

The Wolfe Cycle is a methanogenic pathway used by archaea; the archaeon takes H2 and CO2 and cycles them through a various intermediates to create methane. The Wolfe Cycle is modified in different orders and classes of archaea as per the resource availability and requirements for each species, but it retains the same basic pathway. The pathway begins with the reducing carbon dioxide to formylmethanofuran. The last step uses heterodisulfide reductase (Hdr) to reduce heterodisulfide into Coenzyme B and Coenzyme M using Fe4S4 clusters. Evidence suggests this last step goes hand-in-hand with the first step, and feeds back into it, creating a cycle. At various points in the Wolfe Cycle, intermediates that are formed are taken out of the cycle to be used in other metabolic processes. Since intermediates are being taken out at various points in the cycle, there is also a replenishing (anaplerotic) reaction that feeds into the Wolfe cycle, this is to regenerate necessary intermediates for the cycle to continue. Overall, including the replenishing reaction, the Wolfe Cycle has a total of nine steps. While Obligate reducing methanogens preform additional steps to reduce CO2 to .

References

  1. Thauer RK (September 1998). "Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture". Microbiology. 144 (Pt 9): 2377–406. doi: 10.1099/00221287-144-9-2377 . PMID   9782487.
  2. Vorholt JA, Thauer RK (September 1997). "The active species of CO
    2
    utilized by formylmethanofuran dehydrogenase from methanogenic Archaea"
    . Eur. J. Biochem. 248 (3): 919–24. doi: 10.1111/j.1432-1033.1997.00919.x . PMID   9342247.
  3. Acharya P, Warkentin E, Ermler U, Thauer RK, Shima S (March 2006). "The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes". J. Mol. Biol. 357 (3): 870–9. doi:10.1016/j.jmb.2006.01.015. PMID   16466742.