High affinity cation-binding sites in Complex I from Escherichia coli.
Studies on the activity of Complex I from Escherichia coli in the presence of different metal cations revealed at least two high affinity metal-binding sites. Membrane-bound or isolated Complex I was activated by K(+) (apparent binding constant approximately 125 microM) and inhibited by La(3+) (IC(50)= 1 microM). K(+) and La(3+) do not occupy the same site. Possible localization of these metal-binding sites and their implication in catalysis are discussed.
Euro
Liliya
L
Helsinki Bioenergetics Group, Institute of Biotechnology, PO Box 65 (Viikinkaari 1) 00014 University of Helsinki, Finland. liliya.euro@helsinki.fi
Belevich
Galina
G
Wikström
Mårten
M
Verkhovskaya
Marina
M
D001665:Binding Sites; D002412:Cations / Q000378:metabolism; D042967:Electron Transport Complex I / Q000037:antagonists & inhibitors / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D007811:Lanthanum / Q000378:metabolism / Q000494:pharmacology; D009154:Mutation; D011188:Potassium / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding; D011808:Quinone Reductases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism
D002412:Cations; D029968:Escherichia coli Proteins; D007811:Lanthanum; C502197:NuoF protein, E coli; D011808:Quinone Reductases; D042967:Electron Transport Complex I; D011188:Potassium