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Cited by 502

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N

Jormakka, Mika, Törnroth, Susanna, Byrne, Bernadette, Iwata, So·2002·Science

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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Crossref · 10.1126/science.1068186

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Metadata

Authors
Jormakka, M., Törnroth, S., Byrne, B., & Iwata, S.
Venue
Science
Published
2002-03-08
Volume
295
Issue
5561
Pages
1863-1868
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2057702599
Cited by
502
References
3
FWCI
22.23
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N. https://app.cochat.ai/papers/10.1126/science.1068186
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Jormakka, M., Törnroth, S., Byrne, B., & Iwata, S. (2002). Molecular Basis of Proton Motive Force Generation: Structure of Formate Dehydrogenase-N. Science. https://doi.org/10.1126/science.1068186

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.