1kqf

Structural highlights

Function

[FDNG_ECOLI] Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).^[1] [FDNI_ECOLI] Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).^[2] [FDNH_ECOLI] Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar).^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Formate dehydrogenase 3D structures
• Selenocysteine

References

1. ↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186
2. ↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186
3. ↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186
4. ↑ Jormakka M, Tornroth S, Byrne B, Iwata S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science. 2002 Mar 8;295(5561):1863-8. PMID:11884747 doi:10.1126/science.1068186