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- Title
Response: Commentary: Directions for Optimization of Photosynthetic Carbon Fixation: RuBisCO's Efficiency May Not Be So Constrained After All.
- Authors
Cummins, Peter L.; Kannappan, Babu; Gready, Jill E.
- Abstract
One such enzyme that has been targeted for re-engineering, ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39), is of intensive interest in agriculture and related fields as it fixes CO SB 2 sb in higher plants and the vast majority of other photosynthetic organisms. These results have challenged the accepted view that dissociation of the gas molecules (decarboxylation and deoxygenation) from the enzyme complex is negligible in all wild-type Rubiscos. In a commentary on [1], [20] have contested our conclusion of significant decarboxylation and deoxygenation rates in Rubisco and suggested it is based on a misinterpretation of "implicit relationships between Rubisco rate constants" and "overlooks experimental evidence for feeble rates of deoxygenation and decarboxylation.".
- Subjects
CARBON fixation; RIBULOSE bisphosphate carboxylase; KINETIC isotope effects; ENZYME specificity; ACTIVATION energy
- Publication
Frontiers in Plant Science, 2019, Vol 10, p1
- ISSN
1664-462X
- Publication type
Article
- DOI
10.3389/fpls.2019.01426