CoB—CoM heterodisulfide reductase
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 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=107126.
- 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.