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Rubisco is not really so bad.

Camille Bathellier1, Guillaume Tcherkez1, George H Lorimer2

  • 1Research School of Biology, College of Science, Australian National University, Canberra, 2601, ACT, Australia.

Plant, Cell & Environment
|January 24, 2018
PubMed
Summary
This summary is machine-generated.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is not an inefficient enzyme. This review suggests Rubisco’s catalytic performance is unremarkable, challenging its reputation for slow carbon fixation and highlighting the need for a deeper mechanistic understanding.

Keywords:
CO2carbon reactionscarboxylationcatalytic efficiencyoxygenasephotosynthesisrubisco

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a crucial enzyme in autotrophic organisms, catalyzing CO2 fixation.
  • Despite extensive study, key aspects of Rubisco's catalytic mechanism, particularly its oxygenase activity, remain poorly understood.
  • Rubisco is often perceived as inefficient due to its modest turnover and oxygen inhibition, prompting efforts to enhance its catalytic efficiency.

Purpose of the Study:

  • To re-evaluate Rubisco's catalytic performance by comparing it with chemically related enzymes.
  • To challenge the prevailing view of Rubisco as an inefficient catalyst for CO2 fixation.
  • To provide a new perspective on the oxygenase reaction and its evolutionary context.

Main Methods:

  • Comparative kinetic analysis of Rubisco against other carboxylating and oxygenating enzymes.
  • Re-examination of established data on Rubisco's catalytic properties and mechanism.
  • Literature review and synthesis of current understanding of enzyme mechanisms.

Main Results:

  • Rubisco's catalytic rate is not exceptionally slow when compared to related enzymes.
  • The enzyme's kinetic properties are unremarkable considering the complexity of its reaction.
  • Oxygenation by Rubisco is not an inherent mechanistic outcome but likely a result of evolutionary compromises.

Conclusions:

  • Rubisco's perceived inefficiency may be overstated; its performance is comparable to related enzymes.
  • A more comprehensive understanding of Rubisco's mechanism is needed to explain its CO2/O2 reactivity.
  • Investigating Rubisco's evolutionary trajectory and diversification requires a better grasp of its catalytic strategy and metabolic context.