title: The Mrp Na+/H+ antiporter increases the activity of the malate:quinone oxidoreductase of an Escherichia coli respiratory mutant.
abstract: Mrp catalyzes secondary Na+/H+ antiport and was hypothesized to have an additional primary energization mode. Mrp-dependent complementation of nonfermentative growth of an Escherichia coli respiratory mutant supported this hypothesis but is shown here to be related to increased expression of host malate:quinone oxidoreductase, not to catalytic activity of Mrp.
authors.affiliation: Box 1603, Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.
authors.forename: Talia H
authors.initials: TH
authors.lastname: Swartz
authors.forename: Masahiro
authors.initials: M
authors.lastname: Ito
authors.forename: David B
authors.initials: DB
authors.lastname: Hicks
authors.forename: Mark
authors.initials: M
authors.lastname: Nuqui
authors.forename: Arthur A
authors.initials: AA
authors.lastname: Guffanti
authors.forename: Terry A
authors.initials: TA
authors.lastname: Krulwich
mesh_terms: D002384:Catalysis; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000502:physiology*; D010088:Oxidoreductases / Q000378:metabolism*; D010101:Oxygen Consumption; D017923:Sodium-Hydrogen Exchangers / Q000502:physiology*
chemical_list: D029968:Escherichia coli Proteins; D017923:Sodium-Hydrogen Exchangers; D010088:Oxidoreductases; C471971:malate dehydrogenase, FAD-dependent