PMID:10373108
| Citation |
Iverson, TM, Luna-Chavez, C, Cecchini, G and Rees, DC (1999) Structure of the Escherichia coli fumarate reductase respiratory complex. Science 284:1961-6 |
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| 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. |
| Links | |
| Keywords |
Aerobiosis; Anaerobiosis; Binding Sites; Cell Membrane/enzymology; Crystallization; Crystallography, X-Ray; Electron Transport; Energy Metabolism; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/metabolism; Fumarates/metabolism; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/metabolism; Models, Molecular; Oxidation-Reduction; Oxygen Consumption; Protein Conformation; Protein Folding; Quinones/chemistry; Quinones/metabolism; Succinate Dehydrogenase/chemistry; Succinate Dehydrogenase/metabolism |
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