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.