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- W47731617 abstract "Rubisco (ribulose 1,5-bisphosphate carboxylase/oxygenase) catalyses the CO2 fixation of photosynthesis. Despite its central role for life, Rubisco is inefficient and is subject to competitive inhibition by O2. This makes Rubisco a target for mechanistic studies and engineering, requiring a detailed knowledge of the molecular basis for its catalysis and specificity. Rubisco from higher plants consists of eight large, and eight small subunits. This thesis investigates the role of structural elements of Rubisco, spanning from the active site on the large subunit to the small subunit and the subunit interfaces. The structure of Rubisco with a calcium ion in place of the native magnesium activator ion illustrates how the catalytic properties depend on the nature of the metal ion. The larger radius of the calcium ion and its reduced Lewis-acid character causes increases in certain metal-ligand distances, and could explain why calcium does not support catalysis. The mutation C172S in the active site was shown to simultaneously improve specificity and influence the redox-stability of Rubisco. Analysis of mutations (V331A, T342I) in a mobile loop (Loop 6) of the large subunit illustrates the importance of a precise geometry of the loop for catalytic efficiency and specificity. The substitution D473E at the C-terminus is shown to disrupt a network of hydrogen bonds relayed to Loop 6 and to cause disorder of the C-terminus. This may explain the reduced specificity of this mutant. Mutations at the interface of the large and small subunits also influence the stability and catalytic efficiency. Analysis of temperature factors in the structures of L290F and L290F/A222T pinpoints the regions of instability and suggests how the effect is reversed by one single mutation. The influence of interactions at the subunit interface on catalysis was analysed by replacement of the small-subunit βA-βB loop of Chlamydomonas Rubisco with the corresponding loops of Synechococcus (ABAN) and spinach (ABSO) Rubisco. The structures show a significant interaction area of the βA-βB loop in ABAN is lost, leading to reduced catalytic efficiency and specificity, whereas the total loop-interaction area in ABSO is similar to that in the spinach or wild-type enzymes." @default.
- W47731617 created "2016-06-24" @default.
- W47731617 creator A5005074762 @default.
- W47731617 date "2005-01-01" @default.
- W47731617 modified "2023-09-27" @default.
- W47731617 title "Structure-function studies of ribulose-1,5-bisphosphate carboxylase/oxygenase: activation, thermostability, and CO2/O2 specificity" @default.
- W47731617 hasPublicationYear "2005" @default.
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