6 pp.
6 pp.
| 295 K 6 pp. | |
| View Document | ||
| Title | Chemical and Physical Characterization of the Activation of Ribulosebiphosphate Carboxylase/Oxygenase | |
| Author(s) | Donnelly, M. I.; Ramakrishnan, V.; Hartman, F. C. | |
| Publication Date | August 1983 | |
| Report Number | CONF-8308110-5 | |
| Unique Identifier | ACC0340 | |
| Other Numbers | Legacy ID: DE83017226; OSTI ID: 5776573 | |
| Research Org | Oak Ridge National Laboratory (ORNL), TN (USA) | |
| Contract No | W-7405-ENG-26 | |
| Sponsoring Org | U.S. Department of Energy (DOE), Office of Health and Environmental Research; U.S. Department of Agriculture, Science and Education Administration; National Science Foundation | |
| Other Information | Sixth International Congress on Photosynthesis, Brussels, Belgium, 1 - 6 Aug 1983 | |
| Subject | 59 Basic Biological Sciences; Carboxy-Lyases; Enzyme Activity; Molecular Structure; Rhodospirillum; Spinach; Bacteria; Carbon-Carbon Lyases; Enzymes; Food; Lyases; Microorganisms; Vegetables | |
| Related Web Pages | Venkatraman Ramakrishnan, Thomas A. Steitz, Ada E. Yonath, and Ribosome | |
| Abstract | Molecular structure of ribulosebiphosphate carboxylase/oxygenase isolated from Rhodospirillium was compared with the enzyme isolated from Alcaligens eutrophus. Peptides derived from the active center of the bacterial enzyme were highly homologous with those isolated from spinach. Molecular shapes of the carboxylases were estimated using neutron scattering data. These studies suggested that the enzyme as isolated from R. rubrum is a solid prolate ellipsoid or cylinder, while the spinach enzyme resembles a hollow sphere. | |
| 295 K 6 pp. | |
| View Document | ||
