Coenzyme B

Last updated
Coenzyme B
Coenzyme B (CoB).svg
Names
IUPAC name
2-[(7-mercapto-1-oxoheptyl)amino]-3-phosphonooxybutanoic acid
Identifiers
3D model (JSmol)
ChemSpider
PubChem CID
UNII
  • InChI=1S/C11H22NO7PS/c1-8(19-20(16,17)18)10(11(14)15)12-9(13)6-4-2-3-5-7-21/h8,10,21H,2-7H2,1H3,(H,12,13)(H,14,15)(H2,16,17,18) Yes check.svgY
    Key: JBJSVEVEEGOEBZ-UHFFFAOYSA-N Yes check.svgY
  • InChI=1/C11H22NO7PS/c1-8(19-20(16,17)18)10(11(14)15)12-9(13)6-4-2-3-5-7-21/h8,10,21H,2-7H2,1H3,(H,12,13)(H,14,15)(H2,16,17,18)/t8-,10-/m1/s1
    Key: JBJSVEVEEGOEBZ-PSASIEDQBT
  • InChI=1/C11H22NO7PS/c1-8(19-20(16,17)18)10(11(14)15)12-9(13)6-4-2-3-5-7-21/h8,10,21H,2-7H2,1H3,(H,12,13)(H,14,15)(H2,16,17,18)
    Key: JBJSVEVEEGOEBZ-UHFFFAOYAG
  • O=C(N[C@@H](C(=O)O)[C@H](OP(=O)(O)O)C)CCCCCCS
  • O=C(NC(C(=O)O)C(OP(=O)(O)O)C)CCCCCCS
Properties
C
11
H
22
NO
7
PS
Molar mass 343.333641
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
X mark.svgN  verify  (what is  Yes check.svgYX mark.svgN ?)

Coenzyme B is a coenzyme required for redox reactions in methanogens. The full chemical name of coenzyme B is 7-mercaptoheptanoylthreoninephosphate. [1] The molecule contains a thiol, which is its principal site of reaction.

Coenzyme B reacts with 2-methylthioethanesulfonate (methyl-Coenzyme M, abbreviated CH
3
–S–CoM
), to release methane in methanogenesis: [2]

CH
3
–S–CoM
+ HS–CoB → CH
4
+ CoB–S–S–CoM

This conversion is catalyzed by the enzyme methyl coenzyme M reductase, which contains cofactor F430 as the prosthetic group.

A related conversion that utilizes both HS-CoB and HS-CoM is the reduction of fumarate to succinate, catalyzed by fumarate reductase: [3]

HS–CoM + HS–CoB + O
2
CCH=CHCO
2
O
2
CCH
2
–CH
2
CO
2
+ CoB–S–S–CoM

Importance of Coenzyme B in Methanogenesis

Coenzyme B is an important component in the terminal step of methane biogenesis. [4] It acts as a two electron-donor to reduce coenzyme M (methyl-coenzyme) into two molecules a methane and a heterodisulfide. [5] Two separate experiment that were performed, one with coenzyme B and other without coenzyme B, indicated that using coenzyme B before the formation of the methane molecule, results in a more efficient and consistent bond cleavage. [6]

Related Research Articles

In organic chemistry, a methyl group is an alkyl derived from methane, containing one carbon atom bonded to three hydrogen atoms, having chemical formula CH3. In formulas, the group is often abbreviated as Me. This hydrocarbon group occurs in many organic compounds. It is a very stable group in most molecules. While the methyl group is usually part of a larger molecule, bounded to the rest of the molecule by a single covalent bond, it can be found on its own in any of three forms: methanide anion, methylium cation or methyl radical. The anion has eight valence electrons, the radical seven and the cation six. All three forms are highly reactive and rarely observed.

<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.

<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.

<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

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

<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">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">Sirohydrochlorin</span> Chemical compound

Sirohydrochlorin is a tetrapyrrole macrocyclic metabolic intermediate in the biosynthesis of sirohaem, the iron-containing prosthetic group in sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which catalyzes the release of methane in the final step of methanogenesis.

<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.

<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. Noll KM, Rinehart KL, Tanner RS, Wolfe RS (1986). "Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum". Proceedings of the National Academy of Sciences. 83 (12): 4238–42. Bibcode:1986PNAS...83.4238N. doi: 10.1073/pnas.83.12.4238 . PMC   323707 . PMID   3086878.
  2. 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.
  3. Heim S, Künkel A, Thauer RK, Hedderich R (April 1998). "Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum—identification of the catalytic sites for fumarate reduction and thiol oxidation". European Journal of Biochemistry. 253 (1): 292–9. doi: 10.1046/j.1432-1327.1998.2530292.x . PMID   9578488.
  4. Dey, Mishtu; Li, Xianghui; Kunz, Ryan C; Ragsdale, Stephen W (2010-12-22). "Detection of Organometallic and Radical Intermediates in the Catalytic Mechanism of Methyl-Coenzyme M Reductase Using the Natural Substrate Methyl-Coenzyme M and a Coenzyme B Substrate Analogue". Biochemistry. 49 (51): 10902–10911. doi:10.1021/bi101562m. PMID   21090696.[ permanent dead link ]
  5. Cedervall, Peder E; Dey, Mishtu; Pearson, Arwen R; Ragsdale, Stephen W; Wilmot, Carrie M (2010-07-22). "Structural Insight into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues". Biochemistry. 49 (35): 7683–7693. doi:10.1021/bi100458d. PMC   3098740 . PMID   20707311.
  6. Horng, Yih-Chern; Becker, Donald F; Ragsdale, Stephen W (2001-10-30). "Mechanistic Studies of Methane Biogenesis by Methyl-Coenzyme M Reductase: Evidence that Coenzyme B Participates in Cleaving the C−S Bond of Methyl-Coenzyme M". Biochemistry. 40 (43): 12875–12885. doi:10.1021/bi011196y. PMID   11669624.[ permanent dead link ]