[FeFe] Group A3-hydrogenase
This entry was last updated at: Feb. 9, 2018, 6:46 a.m.
Properties
| Group | [FeFe]-hydrogenases |
| Subgroup | [FeFe] Group A3: Bifurcating |
| Function | Bifurcates electrons from H2 to NAD and ferredoxin. Reverse reaction can also occur resulting in reoxidation of redox carriers concomitant with fermentative H2 evolution. |
| Activity | Electron-bifurcation |
| Oxygen tolerance | O2-labile |
| Localisation | Cytosolic |
Distribution
| Ecosystem distribution | Gastrointestinal tracts, anoxic soils and sediments |
| Taxonomic distribution | Widespread in anaerobic bacteria, including Firmicutes, Bacteroidetes, Deltaproteobacteria, and Spirochaetes |
Genetic Organisation
Organisation 1: Thermotoga maritima (WP_004081677.1):
Organisation 2: Desulfovibrio fructosovorans (WP_005990603.1):
Architecture
| Structures |
|
| Subunits | 3 or 4 |
| Subunit description | HydA (catalytic subunit) HydB (diaphorase subunit) HydC (thioredoxin) In organisation 2, an additional thioredoxin (HydD) is present |
| Catalytic site | [FeFe]-centre |
| FeS clusters | Organisation 1: 3 [4Fe4S] clusters, 2 [2Fe2S] clusters Organisation 2: 3 [4Fe4S] clusters, 1 [2Fe2S] cluster |
Sequences in this class
| NCBI Accession | Organism | Hydrogenase Class | Phylum | Order | Activity (Predicted) | Oxygen Tolerance (Predicted) | Subunits (Predicted) | Metal Centres (Predicted) | Accessory Subunits (Predicted) |
|---|---|---|---|---|---|---|---|---|---|
| WP_005033810.1 | Holophaga foetida | [FeFe] Group A3 | Acidobacteria | Holophagales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_005034114.1 | Holophaga foetida | [FeFe] Group A3 | Acidobacteria | Holophagales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_005038259.1 | Holophaga foetida | [FeFe] Group A3 | Acidobacteria | Holophagales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 2 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_024286588.1 | Cellulomonas sp. KRMCY2 | [FeFe] Group A3 | Actinobacteria | Actinomycetales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_002730048.1 | Phaeospirillum molischianum | [FeFe] Group A3 | Alphaproteobacteria | Rhodospirillales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_014413848.1 | Rhodospirillum photometricum | [FeFe] Group A3 | Alphaproteobacteria | Rhodospirillales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_021133133.1 | Phaeospirillum fulvum | [FeFe] Group A3 | Alphaproteobacteria | Rhodospirillales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_022000256.1 | Acetobacter sp. CAG:977 | [FeFe] Group A3 | Alphaproteobacteria | Rhodospirillales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_022196619.1 | Azospirillum sp. CAG:239 | [FeFe] Group A3 | Alphaproteobacteria | Rhodospirillales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_022418208.1 | Acidiphilium sp. CAG:727 | [FeFe] Group A3 | Alphaproteobacteria | Rhodospirillales | Bifurcating | Labile | 4 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin, thioredoxin |
| WP_026781963.1 | Pleomorphomonas koreensis | [FeFe] Group A3 | Alphaproteobacteria | Rhizobiales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_026791754.1 | Pleomorphomonas oryzae | [FeFe] Group A3 | Alphaproteobacteria | Rhizobiales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_013637757.1 | Desulfurobacterium thermolithotrophum | [FeFe] Group A3 | Aquificae | Desulfurobacteriales | Bifurcating | Labile | 3 | [FeFe]-centre, 2 x [4Fe4S] clusters | NADH dehydrogenase, thioredoxin |
| WP_022847517.1 | Desulfurobacterium sp. TC5-1 | [FeFe] Group A3 | Aquificae | Desulfurobacteriales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_016268012.1 | Bacteroides thetaiotaomicron | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Evolving | Labile | 1 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | None |
| WP_021646890.1 | Bacteroides pyogenes | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Evolving | Labile | 2 | [FeFe]-centre, 2 x [4Fe4S] clusters | Small subunit |
| WP_004319661.1 | Bacteroides ovatus | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_004329321.1 | Alistipes putredinis | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_005643305.1 | Parabacteroides merdae | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_005680505.1 | Bacteroides caccae | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_005836595.1 | Bacteroides uniformis | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_005931733.1 | Bacteroides salyersiae | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_005941255.1 | Bacteroides massiliensis | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_007216264.1 | Bacteroides cellulosilyticus | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_007656765.1 | Parabacteroides goldsteinii | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_008021616.1 | Bacteroides xylanisolvens | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_008157755.1 | Parabacteroides johnsonii | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_009132358.1 | Bacteroides oleiciplenus | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_010537425.1 | Bacteroides faecis | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_010663850.1 | Marinilabilia salmonicolor | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_010665320.1 | Marinilabilia salmonicolor | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_013610540.1 | Odoribacter splanchnicus | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_016777708.1 | Anaerophaga thermohalophila | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_018336996.1 | Butyricimonas synergistica | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_024986193.1 | Bacteroides acidifaciens | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_025863481.1 | Prolixibacter bellariivorans | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_025863484.1 | Prolixibacter bellariivorans | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_025867773.1 | Bacteroides nordii | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_026327676.1 | Proteiniphilum acetatigenes | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_026475062.1 | Alkaliflexus imshenetskii | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_026475073.1 | Alkaliflexus imshenetskii | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 4 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin, thioredoxin |
| WP_027199847.1 | Butyricimonas virosa | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_027326146.1 | Bacteroides pyogenes | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 2 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase |
| WP_027472107.1 | Cytophaga fermentans | [FeFe] Group A3 | Bacteroidetes | Cytophagales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_028729360.1 | Parabacteroides gordonii | [FeFe] Group A3 | Bacteroidetes | Bacteroidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_006928134.1 | Caldithrix abyssi | [FeFe] Group A3 | Caldithrix | Caldithrixales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_010935952.1 | Dehalococcoides mccartyi | [FeFe] Group A3 | Chloroflexi | Dehalococcoidales | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_022849147.1 | Chloroflexi sp. 439 | [FeFe] Group A3 | Chloroflexi | Unclassified | Bifurcating | Labile | 3 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_015424900.1 | Cloacimonas acidaminovorans | [FeFe] Group A3 | Cloacimonetes | Unclassified | Bifurcating | Labile | 1 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin |
| WP_005990603.1 | Desulfovibrio fructosivorans | [FeFe] Group A3 | Deltaproteobacteria | Desulfovibrionales | Bifurcating | Labile | 4 | [FeFe]-centre, 3 x [4Fe4S] clusters, 1 x [2Fe2S] cluster | NADH dehydrogenase, thioredoxin, thioredoxin |
Literature
Genetics:
- Calusinska, M., Happe, T., Joris, B., and Wilmotte, A. (2010) The surprising diversity of clostridial hydrogenases: a comparative genomic perspective. Microbiol. 156: 1575-1588.
- Greening, C., Biswas, A., Carere, C.R., Jackson, C.J., Taylor, M.C., Stott, M.B., Cook, G.M., and Morales, S.E. (2016) Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival. ISME J. 10: 761-777.
- Malki, S., Saimmaime, I., De Luca, G., Rousset, M., Dermoun, Z., and Belaich, J.P., (1995) Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bacteriol. 177: 2628-2636.
- Poudel, S., Tokmina-Lukaszewska, M., Colman, D.R., Refai, M., Schut, G.J., King, P.W., Maness, P.C., Adams, M.W., Peters, J.W., Bothner, B., and Boyd, E.S. (2016) Unification of [FeFe]-hydrogenases into three structural and functional groups. BBA Gen. Subj. 1860: 1910-1921.
- Verhagen, M.F., O'Rourke, T. and Adams, M.W. (1999) The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization. BBA Bioenerg. 1412: 212-229.
- Wolf, P.G., Biswas, A., Morales, S.E., Greening, C., and Gaskins, H.R. (2016) H2 metabolism is widespread and diverse among human colonic microbes. Gut Microb. 7: 235-245.
- Zheng, Y., Kahnt, J., Kwon, I.H., Mackie, R.I., and Thauer, R.K. (2014) Hydrogen formation and its regulation in Ruminococcus albus: involvement of an electron-bifurcating [FeFe]-hydrogenase, of a non-electron-bifurcating [FeFe]-hydrogenase, and of a putative hydrogen-sensing [FeFe]-hydrogenase. J. Bacteriol. 196: 3840-3852.
Physiology:
- Buckel, W. and Thauer, R.K. (2013) Energy conservation via electron bifurcating ferredoxin reduction and proton/Na+ translocating ferredoxin oxidation. BBA Bioenerg. 1827: 94-113.
- Mock, J., Zheng, Y., Mueller, A.P., Ly, S., Tran, L., Segovia, S., Nagaraju, S., Köpke, M., Dürre, P., and Thauer, R.K. (2015) Energy conservation associated with ethanol formation from H2 and CO2 in Clostridium autoethanogenum involving electron bifurcation. J. Bacteriol. 197: 2965-2980.
- Schuchmann, K. and Müller, V. (2014) Autotrophy at the thermodynamic limit of life: a model for energy conservation in acetogenic bacteria. Nat. Rev. Microbiol. 12: 809-821.
- Wang, S., Huang, H., Kahnt, J., and Thauer, R.K. (2013) A reversible electron-bifurcating ferredoxin-and NAD-dependent [FeFe]-hydrogenase (HydABC) in Moorella thermoacetica. J. Bacteriol. 195: 1267-1275.
Biochemistry:
- Caserta, G., Adamska-Venkatesh, A., Pecqueur, L., Atta, M., Artero, V., Roy, S., Reijerse, E., Lubitz, W., and Fontecave, M. (2016) Chemical assembly of multiple metal cofactors: the heterologously expressed multidomain [FeFe]-hydrogenase from Megasphaera elsdenii. BBA Bioenerg. 1857: 1734-1740.
- Losey, N.A., Mus, F., Peters, J.W., Le, H.M., and McInerney, M.J. (2017) Syntrophomonas wolfei uses an NADH-dependent, ferredoxin-independent [FeFe]-hydrogenase to reoxidize NADH. Appl. Environ. Microbiol. 83: e01335-17.
- Schuchmann, K. and Müller, V. (2012) A bacterial electron-bifurcating hydrogenase. J. Biol. Chem. 287: 31165-31171.
- Schut, G.J. and Adams, M.W. (2009) The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J. Bacteriol. 191: 4451-4457.
- Soboh, B., Linder, D., and Hedderich, R. (2004) A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis. Microbiol. 150: 2451-2463.