Uptake and binding of riboflavin by membrane vesicles of Bacillus subtilis.
Riboflavin uptake and membrane-associated riboflavin-binding activity have been investigated in Bacillus subtilis. The uptake and binding activity of the vitamin were found to be repressed coordinately by riboflavin present in the growth medium. The uptake or riboflavin has been shown to have properties of a carrier-mediated process, and membrane vesicles have been shown to demonstrate riboflavin counterflow and exchange. The membrane-associated binding activity for riboflavin has been solubilized with detergents, and a procedure for the partial purification of this component is described. The partially purified riboflavin-binding component has properties expected for a carrier involved in riboflavin uptake, as it shows saturation kinetics and is inhibited by riboflavin analogues. Evidence is also presented showing that reduced riboflavin binds to a greater extent than oxidized riboflavin, and the possible role of the reduced riboflavin in riboflavin uptake is discussed.
D001412:Bacillus subtilis / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D007700:Kinetics; D026901:Membrane Transport Proteins; D010084:Oxidation-Reduction; D012256:Riboflavin / Q000031:analogs & derivatives / Q000302:isolation & purification / Q000378:metabolism*
D002352:Carrier Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D012256:Riboflavin