The quaternary structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco (Nicotiana tabacum) was investigated in solution by means of small angle X-ray scattering. The most important molecular parameters as the radius of gyration (Rg) and the maximum diameter (Dmax) were determined. Both the active and the inactive form of the enzyme were measured at 5 °C and at 20 °C. A more distinct difference in size could be detected between the inactive forms at these two temperatures (Rg = 4.80 nm (5 °C) and 4.68 nm (20 °C)) than between the active forms (Rg = 4.73 nm and 4.69 nm). The maximum diameters were determined to be 13.1 nm for the inactive form at 5 °C and 12.8 nm for the other forms.
A model is proposed consisting of eight large and eight small subunits arranged in the way that seems to be typical for this enzyme in higher plants.
The Quaternary Structure of Bovine alpha-Crystallin. Size and Shape Studies by Sedimentation, Small-angle X-Ray Scattering and Quasi-elastic Light Scattering
