CoB-CoM heterodisulfide reductase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 1.8.98.1
- BRENDA references for 1.8.98.1 (Recommended.)
- PubMed references for 1.8.98.1
- PubMed Central references for 1.8.98.1
- Google Scholar references for 1.8.98.1
- Hedderich R, Berkessel A, Thauer RK (1990). "Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)". Eur. J. Biochem. 193: 255–61. doi:. 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: 2027–32. 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: 10027–39. doi:. 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: 2432–9. doi:. PMID 11034998.

