The nature and alternate rates of the ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) oxygenation intermediate
Conference
·
OSTI ID:221924
Mutant ribulose 1,5-bisphosphate (RuBP) were employed to investigate the partitioning of carbon flow between photosynthesis or photorespiration. Previous functional and structural studies implicate active site Lys329 and Glu48 or R. rubrum RuBp in promoting addition of CO2 to the RuBP-enediol. Two novel O2-dependent side products generated by the K329A and E49Q mutants provided insight into RuBP oxygenase intermediate and roles of Lys329 and Glu48 in oxygenation.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Sponsoring Organization:
- USDOE, Washington, DC (United States)
- DOE Contract Number:
- AC05-96OR22464
- OSTI ID:
- 221924
- Report Number(s):
- CONF-9508202-9; ON: DE96008638
- Resource Relation:
- Conference: 10. international photosynthesis congress, Montpellier (France), 20-25 Aug 1995; Other Information: PBD: [1995]
- Country of Publication:
- United States
- Language:
- English
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