Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.

Article Details

Citation

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.

PubMed ID
11884747 [ View in PubMed
]
Abstract

The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Formate dehydrogenase, nitrate-inducible, major subunitP24183Details
Formate dehydrogenase, nitrate-inducible, iron-sulfur subunitP0AAJ3Details
Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunitP0AEK7Details