ExplorEnz: EC 1.8.98.5

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1.8.98.5

Accepted name:

H₂:CoB-CoM heterodisulfide,ferredoxin reductase

Reaction:

2 reduced ferredoxin [iron-sulfur] cluster + CoB + CoM + 2 H⁺ = 2 H₂ + 2 oxidized ferredoxin [iron-sulfur] cluster + CoM-S-S-CoB

Glossary:

CoB = coenzyme B = N-(7-sulfanylheptanoyl)threonine = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (deprecated)
CoM = coenzyme M = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
CoM-S-S-CoB = CoB-CoM heterodisulfide = N-{7-[(2-sulfoethyl)dithio]heptanoyl}-O³-phospho-L-threonine =
O³-phospho-N-{7-[2-(2-sulfoethyl)disulfan-1-yl]heptanoyl}-L-threonine

Systematic name:

CoB,CoM,ferredoxin:H₂ oxidoreductase

Comments:

This enzyme complex is found in H₂-oxidizing CO₂-reducing methanogenic archaea such as Methanothermobacter thermautotrophicus. It consists of a cytoplasmic complex of HdrABC reductase and MvhAGD hydrogenase. Electron pairs donated by the hydrogenase are transferred via its δ subunit to the HdrA subunit of the reductase, where they are bifurcated, reducing both ferredoxin and CoB-CoM heterodisulfide. The reductase can also form a similar complex with formate dehydrogenase, see EC 1.8.98.6, formate:CoB-CoM heterodisulfide,ferredoxin reductase. cf. EC 1.8.7.3, ferredoxin:CoB-CoM heterodisulfide reductase, EC 1.8.98.4, coenzyme F₄₂₀:CoB-CoM heterodisulfide,ferredoxin reductase, and EC 1.8.98.1, dihydromethanophenazine:CoB-CoM heterodisulfide reductase.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc

References:

1.	Reeve, J.N., Beckler, G.S., Cram, D.S., Hamilton, P.T., Brown, J.W., Krzycki, J.A., Kolodziej, A.F., Alex, L., Orme-Johnson, W.H. and Walsh, C.T. A hydrogenase-linked gene in Methanobacterium thermoautotrophicum strain δ H encodes a polyferredoxin. Proc. Natl. Acad. Sci. USA 86 (1989) 3031–3035. [DOI] [PMID: 2654933]
2.	Hedderich, R., Koch, J., Linder, D. and Thauer, R.K. The heterodisulfide reductase from Methanobacterium thermoautotrophicum contains sequence motifs characteristic of pyridine-nucleotide-dependent thioredoxin reductases. Eur. J. Biochem. 225 (1994) 253–261. [DOI] [PMID: 7925445]
3.	Setzke, E., Hedderich, R., Heiden, S. and Thauer, R.K. H₂: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties. Eur. J. Biochem. 220 (1994) 139–148. [DOI] [PMID: 8119281]
4.	Stojanowic, A., Mander, G.J., Duin, E.C. and Hedderich, R. Physiological role of the F₄₂₀-non-reducing hydrogenase (Mvh) from Methanothermobacter marburgensis. Arch. Microbiol. 180 (2003) 194–203. [DOI] [PMID: 12856108]
5.	Kaster, A.K., Moll, J., Parey, K. and Thauer, R.K. Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc. Natl. Acad. Sci. USA 108 (2011) 2981–2986. [DOI] [PMID: 21262829]
6.	Costa, K.C., Lie, T.J., Xia, Q. and Leigh, J.A. VhuD facilitates electron flow from H₂ or formate to heterodisulfide reductase in Methanococcus maripaludis. J. Bacteriol. 195 (2013) 5160–5165. [DOI] [PMID: 24039260]

[EC 1.8.98.5 created 2017]