Investigations on the Structure and Conformational Dynamics in Ribulose-1,5- Bisphosphate Carboxylase/oxygenase (rubisco) Molecule

A review is made of the published investigations concerning the structure and conformational dynamic changes in the key photosynthetic and photorespiratory enzyme – Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) of higher plants. Recent data on the basis of X-ray crystalography, NMR-spectroscopy, site-directed mutagenesis and other techniques are analysed. Despite some differences in the aminoacid sequence of Rubisco from various species, significant conformational changes are not established. The tertiary and quaternary structure of Rubisco is described in detail emphasizing the active and regulatory sites of the enzyme. Possibilities and limitations of the different methods of studying protein structure and conformation are discussed. Some advantages of the immunochemical methods especially the use of monoclonal antibodies for investigations of dynamic changes of protein structures in solution are pointed out.