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

Jormakka M, Törnroth S, Byrne B, Iwata S
Science 295 1863-8 (2002)
Cited: 215 times
EuropePMC logo PMID: 11884747

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.

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