Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1)

The respiratory protein of the keyhole limpet, Megathura crenulata, the hem ocyanin (KLH), commonly used as an immunogen, binds oxygen cooperatively, w hich implies the existence of different conformations. For the first time, two different conformations of KLH1 were detected upon oxygenation, a deoxy and an oxy state, using small-angle neutron scattering. Rearrangements in the quaternary structure of KLH1 were predicted from the different radii of gyration and the shifts of the minima and maxima in the scattering curves. Upon oxygenation, KLH1 becomes smaller and more compact. Model reconstruct ion of KLH1 indicates a hollow cylinder with two rings located close to bot h ends, which move slightly together upon oxygenation.