| EC |
1.17.5.3 |
| Accepted name: |
formate dehydrogenase-N |
| Reaction: |
formate + a quinone = CO2 + a quinol |
| Other name(s): |
Fdh-N; FdnGHI; nitrate-inducible formate dehydrogenase; formate dehydrogenase N; FDH-N; nitrate inducible Fdn; nitrate inducible formate dehydrogenase |
| Systematic name: |
formate:quinone oxidoreductase |
| Comments: |
The enzyme contains molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters and two heme b groups. Formate dehydrogenase-N oxidizes formate in the periplasm, transferring electrons via the menaquinone pool in the cytoplasmic membrane to a dissimilatory nitrate reductase (EC 1.7.5.1), which transfers electrons to nitrate in the cytoplasm. The system generates proton motive force under anaerobic conditions [3]. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Enoch, H.G. and Lester, R.L. The purification and properties of formate dehydrogenase and nitrate reductase from Escherichia coli. J. Biol. Chem. 250 (1975) 6693–6705. [PMID: 1099093] |
| 2. |
Jormakka, M., Tornroth, S., Byrne, B. and Iwata, S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295 (2002) 1863–1868. [DOI] [PMID: 11884747] |
| 3. |
Jormakka, M., Tornroth, S., Abramson, J., Byrne, B. and Iwata, S. Purification and crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58 (2002) 160–162. [PMID: 11752799] |
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| [EC 1.17.5.3 created 2010 as EC 1.1.5.6, transferred 2017 to EC 1.17.5.3] |
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