Article
Structural and functional consequences of the replacement of proximal residues Cys(172) and Cys(192) in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase from Chlamydomonas reinhardtii.
The Biochemical journal - 15 Apr 2008
García-Murria María-Jesús, Karkehabadi Saeid, Marín-Navarro Julia, Satagopan Sriram, Andersson Inger, Spreitzer Robert J, Moreno Joaquín
Abstract excerpt
Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect...
Topics
- Animals
- Binding Sites
- Catalysis
- Chlamydomonas reinhardtii
- Crystallography, X-Ray
- Cysteine
- Enzyme Stability
- Kinetics
- Models, Molecular
- Mutation
- Protein Structure, Tertiary
- Protein Subunits