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Ribulose 1,5- bisphosphate carboxylase/oxygenase (RuBisCo) is a critical enzyme that catalyzes carbon dioxide assimilation during photosynthesis. However, it is an inefficient enzyme, having an extremely slow catalytic rate. A typical enzyme can process about a thousand molecules per second; however, RuBisCo fixes only around three-carbon dioxides per second. Photosynthetic cells compensate for this slow rate by synthesizing very high amounts of RuBisCo, making it the most abundant single...
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Related Experiment Video

Updated: Apr 28, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
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Oxygen-dependent H2O2 production by Rubisco.

Kangmin Kim1, Archie R Portis

  • 1United States Department of Agriculture, Agricultural Research Service, Photosynthesis Research Unit, USA.

FEBS Letters
|July 29, 2004
PubMed
Summary

Hydrogen peroxide (H2O2) is a byproduct of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activity. Its production rate varies with Rubisco specificity and environmental conditions like temperature.

Area of Science:

  • Biochemistry
  • Enzymology
  • Photosynthesis

Background:

  • Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a key enzyme in photosynthesis.
  • Rubisco's oxygenase activity can lead to photorespiration and reduced photosynthetic efficiency.
  • The production of hydrogen peroxide (H2O2) by Rubisco has been implicated in cellular signaling and oxidative stress.

Purpose of the Study:

  • To investigate and quantify hydrogen peroxide (H2O2) production by various wild-type Rubisco enzymes.
  • To determine the relationship between Rubisco specificity, oxygen/carbon dioxide concentrations, temperature, and H2O2 production.
  • To explore the mechanistic basis of H2O2 generation during Rubisco's oxygenase reaction.

Main Methods:

  • Utilized a sensitive assay to detect and quantify H2O2 production dependent on oxygen and ribulose-1,5-bisphosphate.

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  • Performed parallel assays with varying concentrations of carbon dioxide (CO2) and oxygen (O2).
  • Investigated the effect of high temperature (38°C) on H2O2 production and Rubisco activity.

    • Main Results:

    • Several wild-type Rubisco enzymes were observed to produce H2O2 during oxygen-dependent catalysis.
    • The partitioning of oxygen consumption to H2O2 production by spinach Rubisco was constant (1/260-1/270) under varying CO2/O2.
    • High temperature and lower Rubisco specificity increased H2O2 production rates and partitioning, with *Chlamydomonas reinhardtii* (1/200) and *Rhodospirillum rubrum* (1/150) showing higher partitioning than spinach.

    Conclusions:

    • Rubisco's oxygenase activity directly produces H2O2 via a peroxyketone intermediate.
    • H2O2 production is a conserved feature of Rubisco oxygenation across different species.
    • Factors influencing Rubisco specificity, such as temperature and enzyme evolution, modulate the yield of H2O2, impacting cellular redox balance.