Light-powered CO2 fixation biosystem for the direct biosynthesis of multi-carbon chemicals from CO2

doi:10.1016/S1872-2067(26)64977-7

Abstract

Abstract:

Sustainable biomanufacturing depending on CO₂ conversion contributes to mitigate global dependence on fossil fuels and accelerate a future green economy. However, CO₂ conversion is limited by inefficient CO₂ fixation pathways, deficient capacity for regenerating reducing power and energy, and narrow product scope. Here, a light-powered CO₂ fixation biosystem (LCFB) was developed by coupling a new-to-nature Pyruvate decarboxylase/Malic enzyme (PM) cycle for CO₂ fixation with natural thylakoid membranes for regenerating energy and reducing power. This synthetic LCFB was able to convert CO₂ to organic molecules at a rate of 2.37 nmol min^-1 mg^-1 proteins comparable to that of natural CO₂ fixation system. Further, LCFB was programmed to extend the length of carbon chain for outputting multi-carbon chemicals by designing and constructing multiple anaplerosis CO₂ fixation pathways in a plug-and-play fashion. Finally, the programmed LCFB powered by light facilitated the direct biosynthesis of multi-carbon chemicals from CO₂, such as alcohols, aldehydes, organic acids and amino acids. This study presented here brings a potential avenue for developing a carbon-negative versatile platform to widen the applicability of LCFB and advancing sustainable biomanufacturing in the future.

Key words: Synthetic photosynthesis, Light-powered, CO₂ fixation, Biomanufacturing, Multi-carbon chemicals

Yingying Li, Jian Zhang, Yuxuan Tao, Tiantian Chai, Chunlei Zhao, Xiulai Chen. Light-powered CO₂ fixation biosystem for the direct biosynthesis of multi-carbon chemicals from CO₂[J]. Chinese Journal of Catalysis, 2026, 82: 251-265.

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URL: https://www.cjcatal.com/EN/10.1016/S1872-2067(26)64977-7

https://www.cjcatal.com/EN/Y2026/V82/I3/251

Figures/Tables 6

Fig. 1. Designing LCFB. LCFB consisted of the PM cycle and TKs. Acetaldehyde dehydrogenase (ADH); pyruvate decarboxylase (PDC); malic enzyme (ME), malate thiokinase (MTK); malyl-CoA lyase (MCL); nicotinamide nucleotide transhydrogenase (NNT); photosystem I (PS I); photosystem II (PS II); cytochrome (Cyt); plastoquinone (PQ); plastocyanin (PC); ferredoxin (Fd); ferredoxin NADP+ reductase (FNR).

Fig. 2. Constructing the PM cycle. (A) Schematic representation of the PM cycle for the conversion of CO2. Input module was indicated in red and output module was indicated in blue. acetaldehyde dehydrogenase (ADH); pyruvate decarboxylase (PDC); malic enzyme (ME), malate thiokinase (MTK); malyl-CoA lyase (MCL). (B) Michaelis-Menten kinetics of Acetobacter pasteurianus PDC (ApPDC) for acetaldehyde. (C) Michaelis-Menten kinetics of Clostridium acetobutylicum ME (CcME) for pyruvate. (D) Pyruvate production from acetaldehyde with different PDCs. ApPDC, PDC from Acetobacter pasteurianus, ScPDC, PDC from Saccharomyces cerevisiae, CaPDC, PDC from Clostridium acetobutylicum, ZmPDC, PDC from Zymomonas mobilis. (E) The validation of the input module. EcADH, ADH from Escherichia coli. (F) The validation of the output module. CcME, ME from Clostridium acetobutylicum; McMTK, MTK from Methylococcus capsulatus; MeMCL, MCL from Methylobacterium extorquens. (G) The validation of the PM cycle. (H) The production of glyoxylate in the different PM versions. PM-0: the initial PM cycle before optimization. PM-1: PM-0 with the optimal concentration of enzymes. PM-2: PM-1 with the optimal reaction time.

Fig. 3. Developing LCFB by coupling the PM cycle with TKs. (A) Schematic representation of LCFB for the conversion of CO2 to glyoxylate by coupling the PM cycle with TKs. (B) Steady-state absorption spectrum of TKs isolated from leek, coriander, spinach, kale and lettuce. The absorbance at 470 nm (pale blue thick vertical lines) and 650 nm (salmon pink thick vertical lines) corresponds to Chlb, the absorbance at 495 nm (pale pink thick vertical lines) is from the electron transitions of carotenoids, and the absorbance at 440 nm (yellow thick vertical lines) and 680 nm (lavender thick vertical lines) corresponds to Chla. Chla: chlorophyll a, Chlb: chlorophyll b, Cars: carotenoids. (C) Regulation of ATP production by TKs through light-dark cycles. (D) Regulation of NADPH production by TKs through light-dark cycles. (E) Production of AcCoA and glycolate with TKs. AcCoA, acetyl-CoA. Pink represents the effect of direct ATP addition and TKs-based ATP regeneration on the MTK-catalyzed reaction, respectively; blue represents the effect of direct NADPH addition and TKs-based NADPH regeneration on the GOR-catalyzed reaction, respectively. (F) Synthesis of glyoxylate in LCFBs.

Fig. 4. Programming LCFB to produce C2 compounds. (A) Schematic overview of the light-powered PM-C2 pathway. Glycolate oxidoreductase (GOR), glycolaldehyde dehydrogenase (GDH), acetyl-phosphate synthase (ACPS) and phosphate acetyltransferase (PTA). (B) The production of glycolate by ScGOR (GOR from Saccharomyces cerevisiae), AaGOR (GOR from Acetobacter aceti), NcGOR (GOR from Neurospora crassa). (C) The production of glycolaldehyde by EcGDH (GDH from E. coli), PfGDH (GDH from Pseudomonas fluorescens). (D) The verification of acetyl-CoA with SmACPS and EcPTA by LC-MS. SmACPS, ACPS from Saccharomonospora marina; EcPTA, PTA from E. coli. (E) The validation of the C2 anaplerosis module. (F) The validation of the light-powered PM-C2 pathway. All products were detected in the same reaction mixture containing the light-powered PM-C2 pathway. AcCoA, acetyl-CoA.

Fig. 5. Programming LCFB to produce C3 compounds. (A) Schematic representation of the light-powered PM-C3 pathway. Glyoxylate-aspartate aminotransferase (BhcA) or glyoxylate-alanine aminotransferase (AGX), serine aldolase (LTA) and serine dehydrase (SDA). (B) The production of pyruvate by CnSDA. (C) The production of pyruvate by PaLTA (LTA from Pseudomonas aeruginosa) and CnSDA. (D) The validation of the C3 anaplerosis module with PdBhcA (BhcA from Paracoccus denitrificans) or ScAGX (AGX from S. cerevicae). (E) The validation of the light-powered PM-C3 pathway. All products were detected in the same reaction mixture containing the light-powered PM-C3 pathway.

Fig. 6. Programming LCFB to produce C4 compounds. (A) Schematic overview of the light-powered PM-C4 pathway. Glyoxylate carboligase (GCL), tartronate semialdehyde reductase (TSR), glycerate kinase (GK), enolase (ENO), phosphoenolpyruvate carboxykinase (PCK) and malate dehydrogenase (MDH). (B) Michaelis-Menten kinetics of EcGCL (GCL from E. coli) for glyoxylate. (C) Michaelis-Menten kinetics of AsPCK (PCK from Actinobacillus succinogenes) for PEP (phosphoenolpyruvate). (D) The production of glycerate by GCL and EcTSR in the submodule I. EcGCL, GCL from E. coli; PpGCL, GCL from Pseudomonas putidis. (E) The production of PEP by EcGK (GK from E. coli) and EcENO (ENO from E. coli) in the submodule II. (F) The production of malate by AsPCK and EcMDH (MDH from E. coli) in the submodule III. (G) The validation of the C4 anaplerosis module. (H) The validation of the light-powered PM-C4 pathway. All products were detected in the same reaction mixture containing the light-powered PM-C4 pathway. PEP, phosphoenolpyruvate; OAA, oxaloacetate.

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Light-powered CO₂ fixation biosystem for the direct biosynthesis of multi-carbon chemicals from CO₂

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