Location of the catalytic site of the respiratory fumarate reductase of Escherichia coli.
The location of the catalytic site of the membrane-bound respiratory fumarate reductase of Escherichia coli was investigated using mutants and inhibitors of dicarboxylic acid transport. Comparison of apparent Km and Vmax values for fumarate in intact cells and in inverted membrane vesicles showed that externally added fumarate was required to be transported across the cytoplasmic membrane prior to reduction. The catalytic site of fumarate reductase must therefore be located on the cytoplasmic face of the membrane.
D001224:Aspartic Acid / Q000494:pharmacology; D001665:Binding Sites; D001692:Biological Transport / Q000187:drug effects; D002384:Catalysis; D002462:Cell Membrane / Q000201:enzymology; D003998:Dicarboxylic Acids / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000648:ultrastructure; D007700:Kinetics; D008293:Malates / Q000494:pharmacology; D009097:Multienzyme Complexes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009154:Mutation; D013385:Succinate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013644:Tartrates / Q000494:pharmacology
D003998:Dicarboxylic Acids; D008293:Malates; D009097:Multienzyme Complexes; D013644:Tartrates; D001224:Aspartic Acid; C033727:fumarate reductase complex; D013385:Succinate Dehydrogenase