CoB—CoM heterodisulfide reductase

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CoB—CoM heterodisulfide reductase

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

coenzyme B + coenzyme M + methanophenazine

\rightleftharpoons

N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O₃-phospho-L-threonine + dihydromethanophenazine

The 3 substrates of this enzyme are coenzyme B, coenzyme M, and methanophenazine, whereas its two products are [[N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O₃-phospho-L-threonine]] and dihydromethanophenazine.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other, known, acceptors. The systematic name of this enzyme class is coenzyme B:coenzyme M:methanophenazine oxidoreductase. Other names in common use include heterodisulfide reductase, and soluble heterodisulfide reductase. This enzyme participates in folate biosynthesis.

References

Hedderich R, Berkessel A, Thauer RK (1990). "Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)". Eur. J. Biochem. 193 (1): 255–61. doi:10.1111/j.1432-1033.1990.tb19331.x. PMID 2121478.
Abken HJ, Tietze M, Brodersen J, Baumer S, Beifuss U, Deppenmeier U (1998). "Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Go1". J. Bacteriol. 180 (8): 2027–32. PMC 107126. PMID 9555882.
Simianu M, Murakami E, Brewer JM, Ragsdale SW (1998). "Purification and properties of the heme- and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila". Biochemistry. 37 (28): 10027–39. doi:10.1021/bi9726483. PMID 9665708.
Murakami E, Deppenmeier U, Ragsdale SW (2001). "Characterization of the intramolecular electron transfer pathway from 2-hydroxyphenazine to the heterodisulfide reductase from Methanosarcina thermophila". J. Biol. Chem. 276 (4): 2432–9. doi:10.1074/jbc.M004809200. PMID 11034998.

v t e Oxidoreductases: sulfur oxidoreductases (EC 1.8)
1.8.1: NAD or NADP	Dihydrolipoamide dehydrogenase Glutathione reductase Thioredoxin reductase
1.8.2: cytochrome	Sulfite dehydrogenase Thiosulfate dehydrogenase Flavocytochrome c sulfide dehydrogenase
1.8.3: oxygen	Sulfite oxidase
1.8.4: disulfide	Glutathione—homocystine transhydrogenase
1.8.5: quinone	Glutathione dehydrogenase (ascorbate)
1.8.98: Other, known	CoB—CoM heterodisulfide reductase
1.8.99: Other	Sulfite reductase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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