Mika Jormakka, Susanna Törnroth, Bernadette Byrne, So Iwata
Division of Biomedical Sciences, Imperial College, London SW7 2AZ, UK.
Science (New York, N.Y.) 2002 Mar 8The 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.
Mika Jormakka, Susanna Törnroth, Bernadette Byrne, So Iwata. Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science (New York, N.Y.). 2002 Mar 8;295(5561):1863-8
PMID: 11884747
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