Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is the entry point of CO2 into the Calvin-Benson cycle (CBC), connecting the inorganic carbon and organic carbon realms making it arguably one of the most important enzymes on Earth. Chlamydomonas has proven to be a powerful model for understanding Rubisco biogenesis, function, regulation, and engineering, with this chapter emphasizing core findings in the field of Chlamydomonas Rubisco biology over the last several decades. In addition to performing carboxylation, Rubisco performs an energy wasteful oxygenation reaction that results in photorespiration. To minimize photorespiration, Chlamydomonas operates a highly effective CO2-concentrating mechanism (CCM) that increases the CO2:O2 ratio at the active site of Rubisco, reducing oxygenation of the ribulose-1,5-bisphosphate substrate. The CCM involves an interplay between carbonic anhydrases, inorganic carbon transporters, and structural components to move inorganic carbon against its concentration gradient from the external environment to a specialized subchloroplast structure called the pyrenoid. Rapid advances in understanding CCM function highlighted in this chapter, including recent discoveries concerning the importance of Rubisco structure for its condensation into the pyrenoid, have merged the Rubisco and CCM fields and laid the groundwork for what is expected to be an exciting decade for Rubisco and CCM research.
Published Version
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