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- Title
Structure of the Escherichia coli fumarate reductase respiratory complex.
- Authors
Iverson, T M; Luna-Chavez, C; Cecchini, G; Rees, D C
- 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 bc1.
- Publication
Science (New York, N.Y.), 1999, Vol 284, Issue 5422, p1961
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.284.5422.1961