Photosynthetic CO2 Fixation and Rubisco

Ribbon diagram of hexadecameric Rubisco with large subunits in blue and green and small subunits in yellow. The substrate analogue CABP is shown as red spheres.

Ribbon diagram of hexadecameric Rubisco with large subunits in blue and green and small subunits in yellow. The substrate analogue CABP is shown as red spheres.

Rubisco

The enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is essential for photosynthetic assimilation of CO2 into the biosphere. Rubisco is ubiquitous and is present is plants, algae and certain autotrophic bacteria. The catalytic properties of Rubisco influence crop yield and dictate the efficiency with which plants use their resources of water, nutrients and light. However, the importance of the enzyme is not matched by catalytic excellence. Rubisco is a remarkably inefficient catalyst; it has a low turnover number and it has difficulty distinguishing CO2 from the much more abundant gas, O2. Our research contributes knowledge on several aspects of Rubisco, including the molecular structure, dynamics, catalytic mechanism and subunit interactions.

Ribbon representation of the crystal structure of Rubisco activase from Arabidopsis thaliana rainbow colored from blue in the N-terminus to red in the C-terminus.

Ribbon representation of the crystal structure of Rubisco activase from Arabidopsis thaliana rainbow colored from blue in the N-terminus to red in the C-terminus.

Rubisco activase

As part of a complex regulation, Rubisco is inhibited by formation of dead-end complexes with inhibitory sugar phosphates. In plants and green algae, the ATP-dependent motor protein Rubisco activase restores catalytic competence by facilitating conformational changes in Rubisco, promoting the release of the inhibitory compounds from the active site. Our research aims to study Rubisco activase and its interaction with Rubisco.

Synechococcus elongatus carboxysome shell protein CcmP trimer.

Synechococcus elongatus carboxysome shell protein CcmP trimer.

CO2 concentration and carboxysomes

Rubisco is responsible for fixing an estimated 200 billion tons of CO2 into carbohydrates annually, about half of this in marine phytoplankton. The importance of marine photosynthetic carbon assimilation is paradoxical because the concentration of CO2 in sea water is very low, as a consequence of the slow bulk diffusion of CO2 in water and a relatively high pH value of sea water. Key to the efficiency of marine autotrophs, such as cyanobacteria and chemoautotrophic bacteria, is the ability to encapsulate the CO2-fixing machinery of the cell within a semipermeable protein shell. In these protein compartments called carboxysomes, CO2 is actively concentrated at site of the CO2-fixing enzyme, Rubisco. Our research aims at an understanding of the structure, function and organisation of the carboxysome using different X-ray based methods.

Literature

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year  = {2014},
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}
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title  = "Chimeric Small Subunits Influence Catalysis Without Causing Global",
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title  = "Comparison Of The Crystal-Structures Of L2 And L8S8 Rubisco Suggests A",
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number  = "7",
year  = {1990},
pages  = {2045--2050},
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author  = "Fitchen, Jh and Knight, S and Andersson, I and Branden, Ci and Mcintosh, L",
title  = "Residues In 3 Conserved Regions Of The Small Subunit Of",
journal  = "Proceedings Of The National Academy Of Sciences Of The United States Of",
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number  = "15",
doi  = {10.1073/pnas.87.15.5768},
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title  = "Crystallographic Analysis Of Ribulose 1,5-Bisphosphate Carboxylase From",
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author  = "Andersson, I and Knight, S and Schneider, G and Lindqvist, Y and Lundqvist, T and Branden, Ci and Lorimer, Gh",
title  = "Crystal-Structure Of The Active-Site Of Ribulose-Bisphosphate",
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author  = "Knight, S and Andersson, I and Branden, Ci",
title  = "Reexamination Of The 3-Dimensional Structure Of The Small Subunit Of",
journal  = "Science",
volume  = "244",
number  = "4905",
doi  = {10.1126/science.244.4905.702},
year  = {1989},
pages  = {702--705},
}
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    @ARTICLE{17,
author  = "Branden, Ci and Schneider, G and Lindqvist, Y and Andersson, I and Knight, S and Lorimer, Gh",
title  = "X-Ray Structural Studies Of Rubisco From Rhodospirillum-Rubrum And",
journal  = "Philosophical Transactions Of The Royal Society Of London Series",
volume  = "313",
number  = "1162",
doi  = {10.1098/rstb.1986.0043},
year  = {1986},
pages  = {359--&},
}
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    @ARTICLE{18,
author  = "Andersson, I and Branden, Ci",
title  = "Large Single-Crystals Of Spinach 1,5-Bisphosphate Carboxylase Oxygenase",
journal  = "Journal Of Molecular Biology",
volume  = "172",
number  = "3",
doi  = {10.1016/S0022-2836(84)80033-9},
year  = {1984},
pages  = {363--366},
}
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    @ARTICLE{19,
author  = "Andersson, I and Tjader, Ac and Cedergrenzeppezauer, E and Branden, Ci",
title  = "Crystallization And Preliminary-X-Ray Studies Of Spinach Ribulose",
journal  = "Journal Of Biological Chemistry",
volume  = "258",
number  = "23",
year  = {1983},
pages  = {4088--4090},
}