Role of carboxysomes in cyanobacterial <scp> CO <sub>2</sub> </scp> assimilation: <scp> CO <sub>2</sub> </scp> concentrating mechanisms and metabolon implications
Clair A. Huffine, Runyu Zhao, Yinjie Tang, Jeffrey C. Cameron
Abstract
Abstract Many carbon‐fixing organisms have evolved CO 2 concentrating mechanisms (CCMs) to enhance the delivery of CO 2 to RuBisCO, while minimizing reactions with the competitive inhibitor, molecular O 2 . These distinct types of CCMs have been extensively studied using genetics, biochemistry, cell imaging, mass spectrometry, and metabolic flux analysis. Highlighted in this paper, the cyanobacterial CCM features a bacterial microcompartment (BMC) called ‘carboxysome’ in which RuBisCO is co‐encapsulated with the enzyme carbonic anhydrase (CA) within a semi‐permeable protein shell. The cyanobacterial CCM is capable of increasing CO 2 around RuBisCO, leading to one of the most efficient processes known for fixing ambient CO 2 . The carboxysome life cycle is dynamic and creates a unique subcellular environment that promotes activity of the Calvin–Benson (CB) cycle. The carboxysome may function within a larger cellular metabolon, physical association of functionally coupled proteins, to enhance metabolite channelling and carbon flux. In light of CCMs, synthetic biology approaches have been used to improve enzyme complex for CO 2 fixations. Research on CCM‐associated metabolons has also inspired biologists to engineer multi‐step pathways by providing anchoring points for enzyme cascades to channel intermediate metabolites towards valuable products.