Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic red algae with a strong specificity for CO2 fixation

Biochem Biophys Res Commun. 1997 Apr 17;233(2):568-71. doi: 10.1006/bbrc.1997.6497.

Abstract

Strongly carboxylase-specific ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) was found in Galdieria partita and Cyanidium caldarium (Cyanidiophyceae). The relative specificity, VcKo/VoKc, of Galdieria and Cyanidium RuBisCO was 238 and 222, respectively; 2.4 to 2.5-fold that of higher plant RuBisCOs. The apparent Km of RuBisCO from the thermophilic red algae for CO2 was 6 to 7 microM and the smallest of the values reported so far for other RuBisCOs. The pre-rhodophyte Porphiridium purpureum, which lives at moderate temperatures, had RuBisCO with the relative specificity value of 144. A large difference (5.2 kcal x mol(-1)) in the activation energies between the carboxylase and oxygenase activities in Galdieria RuBisCO was a cause of the strong specificity for the carboxylase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Dioxide / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Kinetics
  • Rhodophyta / enzymology*
  • Ribulose-Bisphosphate Carboxylase / metabolism*
  • Substrate Specificity

Substances

  • Carbon Dioxide
  • Ribulose-Bisphosphate Carboxylase