Year: 2023
Type: review
Abstract: Carbon fixation is the process by which CO2 is converted from a gas into biomass. The Calvin–Benson–Bassham cycle (CBB) is the dominant carbon-consuming pathway on Earth, driving >99.5% of the ∼120 billion tons of carbon that are converted to sugar by plants, algae, and cyanobacteria. The carboxylase enzyme in the CBB, ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco), fixes one CO2 molecule per turn of the cycle into bioavailable sugars. Despite being critical to the assimilation of carbon, rubisco's kinetic rate is not very fast, limiting flux through the pathway. This bottleneck presents a paradox: Why has rubisco not evolved to be a better catalyst? Many hypothesize that the catalytic mechanism of rubisco is subject to one or more trade-offs and that rubisco variants have been optimized for their native physiological environment. Here, we review the evolution and biochemistry of rubisco through the lens of structure and mechanism in order to understand what trade-offs limit its improvement. We also review the many attempts to improve rubisco itself and thereby promote plant growth.
Source: Annual Review of Biochemistry
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Awards: Mapping sequence-function landscapes to isolate improved variants of the dominant carbon-fixing enzyme, TAS::89 0331::TAS RECOVERY RECOVERY ACT BLOCK GRANT FOR ARRA FUNDING. NEW AWARD FOR OFFICE OF STRATEGIC PLANNING FOR WASHTENAW, MI., G6298335418, MECHANISMS OF SELF-ASSEMBLY AND CATALYSIS IN PROTEIN MICROCOMPARTMENTS, Synthetic biology and organelle genomics: A rubisco library as a case study in evolutionary landscapes and organellar engineering
OpenAlex ID: W4367040802