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 126.96.36.199), which transfers electrons to nitrate in the cytoplasm. The system generates proton motive force under anaerobic conditions .
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]
Jormakka, M., Tornroth, S., Byrne, B. and Iwata, S. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science295 (2002) 1863–1868. [DOI] [PMID: 11884747]
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]
[EC 188.8.131.52 created 2010 as EC 184.108.40.206, transferred 2017 to EC 220.127.116.11]