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Structure of the Escherichia coli Fumarate Reductase Respiratory Complex

Iverson, Tina M. and Luna-Chavez, César and Cecchini, Gary and Rees, Douglas C. (1999) Structure of the Escherichia coli Fumarate Reductase Respiratory Complex. Science, 284 (5422). pp. 1961-1966. ISSN 0036-8075. doi:10.1126/science.284.5422.1961.

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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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Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 1999 American Association for the Advancement of Science. Received 3 May 1999; accepted 21 May 1999. Supported by the Department of Veterans Affairs, NIH, and NSF (G.C. and C.L-C.), and the Howard Hughes Medical Institute and NIH (D.C.R.). T.M.I. is supported by an NIH training grant. We thank I. Schröder, S. I. Chan, S. C. Hung, and the members of the Rees group for discussions; K. H. Tubman and T. D. Tubman for critical reading; and J. J. Ottesen and T. N. Earnest for experimental assistance. The Advanced Light Source is supported by the Director, Office of Energy Research, Office of Basic Energy Sciences, Materials Sciences Division, of the U.S. Department of Energy under Contract No. DE-AC03-76SF00098 at Lawrence Berkeley National Laboratory.
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Department of Veterans AffairsUNSPECIFIED
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Department of Energy (DOE)DE-AC03-76SF00098
Issue or Number:5422
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:52089
Deposited By: Tony Diaz
Deposited On:24 Nov 2014 21:29
Last Modified:10 Nov 2021 19:20

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