The Mrp Na+/H+ antiporter increases the activity of the malate:quinone oxidoreductase of an Escherichia coli respiratory mutant.
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.
Swartz
Talia H
TH
Box 1603, Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, 1 Gustave L. Levy Place, New York, NY 10029, USA.
Ito
Masahiro
M
Hicks
David B
DB
Nuqui
Mark
M
Guffanti
Arthur A
AA
Krulwich
Terry A
TA
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*
D029968:Escherichia coli Proteins; D017923:Sodium-Hydrogen Exchangers; D010088:Oxidoreductases; C471971:malate dehydrogenase, FAD-dependent