Biology:F420H2DH family
| Identifiers | |
|---|---|
| Symbol | F420H2DH |
| TCDB | 3.D.9 |
The H+-translocating F420H2 Dehydrogenase (F420H2DH) Family (TC# 3.D.9) is a member of the Na+ transporting Mrp superfamily. A single F420H2 dehydrogenase (also referred to as F420H2:quinol oxidoreductase) from the methanogenic archaeon, Methanosarcina mazei Gö1, has been shown to be a redox driven proton pump. The F420H2DH of M. mazei has a molecular size of about 120 kDa and contains Fe-S clusters and FAD. A similar five-subunit enzyme has been isolated from Methanolobus tindarius. The sulfate-reducing Archaeoglobus fulgidus (and several other archaea) also have this enzyme.[1]
Function
Reduction of 2-hydroxyphenazine by F420H2DH is accompanied by the translocation of 1 H+ per 2 electrons transferred.
Transport Reaction
The overall vectorial reaction catalyzed by F420H2DH is
- Reduced donor (2e−) + H+ (in) ⇌ oxidized acceptor (2e−) + H+ (out)
Role in Methanogenesis
Methanomassiliicoccus luminyensis has been isolated from the human gut and requires H2 and methanol or methylamines to produce methane. The organism lacks cytochromes, indicating that it cannot couple membrane-bound electron transfer reactions with the extrusion of protons or sodium ions using other known methanogenic pathways. Furthermore, M. luminyensis contains a soluble MvhAGD/HdrABC complex, as found in obligate hydrogenotrophic methanogens, but the energy conserving methyltransferase (MtrA-H) is absent.[2][3] Evidence has been presented that M. luminyensis uses two types of heterodisulfide reductases (HdrABC and HdrD) in an energy conserving process.[4] RT-qPCR studies revealed that genes coding for both heterodisulfide reductases were expressed at high levels.[4] Other genes with high transcript abundance were fpoA as part of the operon encoding the 'headless' F420H2 dehydrogenase and atpB as part of the operon encoding the A1Ao ATP synthase. High activities of the soluble heterodisulfide reductase HdrABC and the hydrogenase MvhADG were found in the cytoplasm. Also, heterologously produced HdrD could reduce CoM-S-S-CoB using reduced methylviologen as electron donor. It is proposed that membrane-bound electron transfer is based on the conversion of two molecules of methanol and the concurrent formation of two molecules of the heterodisulfide CoM-S-S-CoB.[4] First, the HdrABC/MvhADG complex catalyzes the H2-dependent reduction of CoM-S-S-CoB and the formation of reduced ferredoxin. Second, reduced ferredoxin is oxidized by the 'headless' F420H2 dehydrogenase, thereby translocating up to 4 H+ across the membrane, and electrons are channeled to HdrD for the reduction of the second heterodisulfide.[4]
Homology
The gene cluster encoding the F420H2DH includes 12 genes, fpoABCDHIJKLMNO. Several of the subunits are related to those of the mitochondrial 'complex I' NDH family members (TC# 3.D.1). Thus, the gene products, FpoA, H, J, K, L, M and N, are highly hydrophobic and are homologous to subunits that form the membrane integral module of NDH-1. FpoB, C, D and I have their counterparts in the amphipathic membrane-associated module of NDH-1. However, homologues of the hydrophilic subunits of the NADH-oxidizing complex are absent.[5]
See also
References
- ↑ "The F420H2 dehydrogenase from Methanosarcina mazei is a Redox-driven proton pump closely related to NADH dehydrogenases". The Journal of Biological Chemistry 275 (24): 17968–73. June 2000. doi:10.1074/jbc.M000650200. PMID 10751389.
- ↑ "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by genome-centric metagenomics". Science 350 (6259): 434–8. October 2015. doi:10.1126/science.aac7745. PMID 26494757. Bibcode: 2015Sci...350..434E.
- ↑ "Bioenergetics and anaerobic respiratory chains of aceticlastic methanogens". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1837 (7): 1130–47. July 2014. doi:10.1016/j.bbabio.2013.12.002. PMID 24333786.
- ↑ 4.0 4.1 4.2 4.3 "Evidence for the involvement of two heterodisulfide reductases in the energy-conserving system of Methanomassiliicoccus luminyensis". The FEBS Journal 283 (3): 472–83. February 2016. doi:10.1111/febs.13594. PMID 26573766.
- ↑ "Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I". Science 347 (6217): 44–9. January 2015. doi:10.1126/science.1259859. PMID 25554780. http://publikationen.ub.uni-frankfurt.de/files/44770/Zickermann_et_al_Zweitveroeffentlichung.pdf.
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