References
The data from Uppsala, which relates mechanism
and X-ray structure
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Structure and mechanism:The data from Uppsala, which relates mechanism and X-ray structure: [top] Andersson, I. and Taylor, T. C. (1997). The Structure of the Complex between Rubisco and its Natural Substrate Ribulose 1,5-Bisphosphate. J. Mol. Biol. 265, 432-444. Andersson, I. and Taylor, T. C. (1997). Structure of a Product Complex of Spinach Ribulose-1,5-bisphosphate Carboxylase/Oxygenase. Biochemistry, 36, 4041-4046. Andersson, I. and Taylor, T. C. Structural transitions during activation and ligand binding in hexadecameric Rubisco inferred from the crystal structure of the activated unliganded spinach enzyme. (1996). Nature Struct. Biol. 3, 95-101. Andersson, I. Large Structures at High Resolution: The 1.6Å Crystal Structure of Spinach Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Complexed with 2-Carboxyarabinitol Bisphosphate. (1996). J. Mol. Biol. 259, 160-174. Of special interest for mechanism and stereochemistry (dealing at length with the remarkable role of carbamate) -- [but not accessible even in abstract unless you subscribe?]: [top] Cleland, W. W., Andrews, J., Gutteridge, S., Hartman, F. C. and Lorimer G. H. (1998). Mechanism of Rubisco: The Carbamate as General Base. Chem. Rev. 98, 549-561. [Note that fig 2 of that article seems to have been inserted into the text without updating the numbering for some of the remaining diagrams; on casual perusal this may cause confusion.] An ab initio examination of the active site and detailed consideration of the role of carbamate: [top] King, W. A., Gready, J. E. and Andrews, T. J. (1998). Quantum chemical analysis of the enolisation of ribulose-bisphosphate: the first hurdle in the fixation of CO2 by Rubisco. Biochemistry. 44, 15414-15422. Mauser H, King WA, Gready JE, Andrews TJ. Site Directed Mutagensis. The proposed mechanism of Rubisco has been constrained by an enormous number of carefully designed sdm experiments; the following give a flavour of recent research in this area. Larimer, F.W., Harpel, M. R. and Hartman, F. C. (1994). Beta-elimination of phosphate from reaction intermediates by site-directed mutants of ribulose-bisphosphate carboxylase/oxygenase. J. Biol. Chem. 269 (15), 11114-20. Bainbridge, G., Andralojc, P. J., Madgwick, P. J. Pitts, J. E. and Parry, M. A. J. (1998). Effect of mutation of lysine-128 of the large subunit of ribulose bisphosphate carboxylase/oxygenase from Anacystis nidulans. Biochem. J. 336 (2), 387-93. Larson, E. M., Larimer, F. W. and Hartman, F. C. (1995). Mechanistic insights provided by deletion of a flexible loop at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase. Biochemistry. 34 (14), 4531-7. Wider context and historical perspective: [top]Schneider, G., Lindqvist, Y. and Brändén, C. (1992). RUBISCO: Structure and Mechanism. Annu. Rev. Biophys. Biomol. Struct. 21, 119-143. Hartman, F. C. and Harpel, M. R. (1994). Structure, function, regulation and assembly of D-Ribulose-1,5-bishosphate carboxylase/oxygenase. Annu. Rev. Biochem. 63, 197-234. Parry, M. A. J., Loveland, J. E. and Andralojc, P. J. (1999). Regulation of Rubisco. Plant Carbohydrate Biochemistry. Ed. Bryant, J. A., Burrell, B. M. M. and Kruger, N. J. BIOS Scientific Publishers Ltd. Oxford. Ellis, R. J. (1979). The most abundant protein in the world. TIBS. November 1979, 241-244. Knaff, D. B. (1989). Structure and regulation of ribuolose-1,5-bisphosphate carboxylase/oxygenase. TIBS. May 1989, 159-160. Some more recent papers of special interest: [top] News Focus: Genetic engineers aim to soup up crop synthesis. Science. 283, 314-316. An excellent insight into the aspirations of scientists involved in genetic engineering. Sugawara, H., Yamamoto, H., Shibata, N., Inoue,T., Okada, S., Miyake,C., Yokota, A. and Yasushi, K. (1999) . Crystal Structure of Carboxylase Reaction-oriented Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from a Thermophilic Red Alga, Galdieria partita. J. Biol. Chem. 274 (22), 15655-15661 Ezaki, S., Maeda, N., Kishimoto, T., Atomi, H. and Imanaka, T. (1999). Presence of a Structurally Novel Type Ribulose-bisphosphate Carboxylase/Oxygenase in the Hyperthermophilic Archaeon, Pyrococcus kodakaraensis KOD1. J. Biol. Chem. 274 (8), 5078-5082 Watson, G. M. F., Yu, J. and Tabita, F. R. (1999). Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic Archaea. J. Bacteriol. 181(5), 1569-75.
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Last updated March 2003 |
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