Rebekka M. Wachter
Research
Regulation of carbon fixation in higher plants
and green algae
Enzymatic turnover of RuBisCo (ribulose 1,5-bisphosphate
caboxylase/oxygenase) is the rate-determining process in
biological carbon fixation, as this enzyme utilizes atmospheric
CO2 to catalyze the carboxylation of a five-carbon sugar.  The
ensuing products are fed directly into the Calvin cycle for the
biosynthesis of more complex carbohydrates.  RuBisCo is
common to all photosynthetic organisms and is arguably the
most abundant protein on Earth.
Department of Chemistry and Biochemistry
Center for Bioenergy and Photosynthesis
 However, the net rate of biological carbon sequestration (and therefore the net rate of
photosynthesis) is limited by the relatively slow catalytic rate of RuBisCo.  In plants adapted to
temperate climates, photosynthesis has been shown to decrease under moderate heat stress (>35°
C), leading to far-reaching environmental and agricultural consequences.  This effect is of particular
concern, as models of global climate change predict a gradual increase in CO2 concentration in the
Earth’s atmosphere over the next few decades, and the elevation of this greenhouse gas appears to
be linked to rising global temperatures.  Auxiliary factors play an essential role in maintaining
RuBisCo activity in live cells.  Some of these proteins have been demonstrated to be indispensable
for plants to stay alive and thrive.  
Bioenergy
In green plants, moderate heat
stress leads to a tremendous
decrease in net
photosynthesis.