The shape of ribulose bisphosphate carboxylase/oxygenase in solution as inferred from small angle neutron scattering

Small angle neutron scattering of both activated and deactivated hexadecameric ribulose bisphosphate carboxylase/oxygenase from spinach revealed that its structure in solution very closely resembles that determined for the deactivated crystalline enzyme from tobacco (Baker, T.S., Eisenberg, D., and Eiserling, F. (1977) Science 196, 293-295). Scattering from both forms of the enzyme in H2O most closely fits that expected from a hollow sphere with an outer radius of 56.4 A and inner radius of 14.3 A. In D2O the enzyme's scattering profiles more closely resembled those of a hollow cylinder with an axial ratio of approximately 1.06 and outer and inner radii of 46.7 and 12.9 A, respectively. Superpositioning of model structures showed that both models determined by neutron scattering correspond quite well to that inferred from x-ray diffraction and electron microscopy of the tobacco enzyme. Sedimentation velocity studies confirmed that no major conformational change occurs upon activation of the spinch carboxylase, both forms exhibiting a sedimentation coefficient, 8(20,w), of 17.8 S. Neutron scattering by activated and deactivated carboxylase from Rhodospirillum rubrum, a dimeric enzyme, best matched that predicted for a solid prolate ellipsoid or cylinder. The estimated dimensions of the model structures correspond strikingly well to those predicted for adjacent pairs of large subunits in the hexadecameric tobacco enzyme.