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Cited by 416

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Structure of the Escherichia coli Fumarate Reductase Respiratory Complex

Iverson, Tina M., Luna-Chavez, César, Cecchini, Gary, Rees, Douglas C.·1999·Science

Abstract

The integral membrane protein fumarate reductase catalyzes the final step of anaerobic respiration when fumarate is the terminal electron acceptor. The homologous enzyme succinate dehydrogenase also plays a prominent role in cellular energetics as a member of the Krebs cycle and as complex II of the aerobic respiratory chain. Fumarate reductase consists of four subunits that contain a covalently linked flavin adenine dinucleotide, three different iron-sulfur clusters, and at least two quinones. The crystal structure of intact fumarate reductase has been solved at 3.3 angstrom resolution and demonstrates that the cofactors are arranged in a nearly linear manner from the membrane-bound quinone to the active site flavin. Although fumarate reductase is not associated with any proton-pumping function, the two quinones are positioned on opposite sides of the membrane in an arrangement similar to that of the Q-cycle organization observed for cytochrome bc 1 .

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Crossref · 10.1126/science.284.5422.1961

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Metadata

Authors
Iverson, T. M., Luna-Chavez, C., Cecchini, G., & Rees, D. C.
Venue
Science
Published
1999-06-18
Volume
284
Issue
5422
Pages
1961-1966
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2093007887
Cited by
416
References
5
FWCI
30.02
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Structure of the Escherichia coli Fumarate Reductase Respiratory Complex. https://app.cochat.ai/papers/10.1126/science.284.5422.1961
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Iverson, T. M., Luna-Chavez, C., Cecchini, G., & Rees, D. C. (1999). Structure of the Escherichia coli Fumarate Reductase Respiratory Complex. Science. https://doi.org/10.1126/science.284.5422.1961

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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.