Rubisco is not really so bad
Date
2018-01-23
Authors
Bathellier, Camille
Tcherkez, Guillaume
Lorimer, George H.
Farquhar, Graham
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Volume Title
Publisher
Blackwell Publishing Ltd
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the most widespread carboxylating enzyme in autotrophic organisms. Its kinetic and structural properties have been intensively studied for more than half a century. Yet important aspects of the catalytic mechanism remain poorly understood, especially the oxygenase reaction. Because of its relatively modest turnover rate (a few catalytic events per second) and the competitive inhibition by oxygen, Rubisco is often viewed as an inefficient catalyst for CO2 fixation. Considerable efforts have been devoted to improving its catalytic efficiency, so far without success. In this review, we re-examine Rubisco's catalytic performance by comparison with other chemically related enzymes. We find that Rubisco is not especially slow. Furthermore, considering both the nature and the complexity of the chemical reaction, its kinetic properties are unremarkable. Although not unique to Rubisco, oxygenation is not systematically observed in enolate and enamine forming enzymes and cannot be considered as an inevitable consequence of the mechanism. It is more likely the result of a compromise between chemical and metabolic imperatives. We argue that a better description of Rubisco mechanism is still required to better understand the link between CO2 and O2 reactivity and the rationale of Rubisco diversification and evolution.
Description
Keywords
CO2, carbon reactions, carboxylation, catalytic efficiency, oxygenase, photosynthesis, rubisco
Citation
Bathellier C, Tcherkez G, Lorimer GH, Farquhar GD. Rubisco is not really so bad. Plant Cell Environ. 2018;41:705–716. https://doi.org/10.1111/pce.13149
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Source
Plant Cell and Environment
Type
Journal article
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Open Access
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Author Accepted Manuscript