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Science 18 June 1999:
Vol. 284. no. 5422, pp. 1961 - 1966
DOI: 10.1126/science.284.5422.1961
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Research Articles

Structure of the Escherichia coli Fumarate Reductase Respiratory Complex

Tina M. Iverson, 1 César Luna-Chavez, 2 Gary Cecchini, 2* Douglas C. Rees 3*

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 bc1.

1 Graduate Option in Biochemistry, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.
2 Molecular Biology Division, Department of Veterans Affairs Medical Center, San Francisco, CA 94121, and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.
3 Howard Hughes Medical Institute, Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.
*   To whom correspondence should be addressed. E-mail: ceccini{at}itsa.ucsf.edu; dcrees{at}caltech.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)