Structural and functional analyses of Rubisco from arctic diatom species reveal unusual posttranslational modifications.

ABSTRACT: The catalytic performance of the major CO₂-assimilating enzyme, ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), restricts photosynthetic productivity. Natural diversity in the catalytic properties of Rubisco indicates possibilities for improvement. Oceanic phytoplankton contain some of the most efficient Rubisco enzymes, and diatoms in particular are responsible for a significant proportion of total marine primary production as well as being a major source of CO₂ sequestration in polar cold waters. Until now, the biochemical properties and three-dimensional structures of Rubisco from diatoms were unknown. Here, diatoms from arctic waters were collected, cultivated, and analyzed for their CO₂-fixing capability. We characterized the kinetic propert

SUBMITTER: Valegard K 

PROVIDER: S-EPMC6109933 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature