Rubisco carboxylase/oxygenase: From the enzyme to the globe: A gas exchange perspective.

J Plant Physiol

Australian Research Council Centre of Excellence for Translational Photosynthesis, Division of Plant Science, Research School of Biology, The Australian National University, Acton, Australian Capital Territory, 2601, Australia. Electronic address:

Published: September 2020

Rubisco is the primary carboxylase of the photosynthetic process, the most abundant enzyme in the biosphere, and also one of the best-characterized enzymes. Rubisco also functions as an oxygenase, a discovery made 50 years ago by Bill Ogren. Carboxylation of ribulose bisphosphate (RuBP) is the first step of the photosynthetic carbon reduction cycle and leads to the assimilation of CO, whereas the oxygenase activity necessitates the recycling of phosphoglycolate through the photorespiratory carbon oxidation cycle with concomitant loss of CO. Since the discovery of Rubisco's dual function, the biochemical properties of Rubisco have underpinned the mechanistic mathematical models of photosynthetic CO fixation which link Rubisco kinetic properties to gas exchange of leaves. This has allowed assessments of global CO exchange and predictions of how Rubisco has and will shape the environmental responses of crop and global photosynthesis in future climates. Rubisco's biochemical properties, including its slow catalytic turnover and poor affinity for CO, constrain crop growth and therefore improving its activity and regulation and minimising photorespiration are key targets for crop improvement.

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Source
http://dx.doi.org/10.1016/j.jplph.2020.153240DOI Listing

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