The nature and alternate rates of the ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) oxygenation intermediate

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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.

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5 p.

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Harpel, M.R.; Chen, Yuh-Ru & Hartman, F.C. December 31, 1995.

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Description

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.

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5 p.

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OSTI as DE96008638

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  • 10. international photosynthesis congress, Montpellier (France), 20-25 Aug 1995

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  • Other: DE96008638
  • Report No.: CONF-9508202--9
  • Grant Number: AC05-96OR22464
  • Office of Scientific & Technical Information Report Number: 221924
  • Archival Resource Key: ark:/67531/metadc668422

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  • December 31, 1995

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  • June 29, 2015, 9:42 p.m.

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  • Jan. 19, 2016, 8:25 p.m.

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Harpel, M.R.; Chen, Yuh-Ru & Hartman, F.C. The nature and alternate rates of the ribulose 1,5-bisphosphate (RuBP) carboxylase/oxygenase (Rubisco) oxygenation intermediate, article, December 31, 1995; Tennessee. (digital.library.unt.edu/ark:/67531/metadc668422/: accessed December 14, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.