Chinese Journal of Catalysis ›› 2026, Vol. 83: 198-208.DOI: 10.1016/S1872-2067(25)64905-9
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Jian Zhanga,1, Yamei Gana,1, Pan Zhub,1, Zihan Zhaoa, Xiulai Chena,*(
)
Received:2025-08-05
Accepted:2025-09-26
Online:2026-04-18
Published:2026-03-04
Contact:
Xiulai Chen
About author:First author contact:1Contributed equally to this work.
Supported by:Jian Zhang, Yamei Gan, Pan Zhu, Zihan Zhao, Xiulai Chen. Light-driven conversion of one-carbon compounds to achieve energy-efficient production of chemicals[J]. Chinese Journal of Catalysis, 2026, 83: 198-208.
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URL: https://www.cjcatal.com/EN/10.1016/S1872-2067(25)64905-9
Fig. 1. Designing LDBS for C1 utilization. LDBS consisted of reducing power regeneration and C1 fixation modules. Reducing power regeneration module was constructed by biosynthesizing CdSe QDs to enable the conversion of solar energy to reducing power. C1 fixation module was built by installing new-to-nature C1-fixing pathways for C1 utilization in E. coli. By coupling reducing power regeneration and C1 fixation modules, LDBS could be designed to capture solar energy for regenerating reducing power, and then reducing power could be utilized to drive the conversion of C1 compounds for bioproduction. e?: electron; Dred: reduced electron donor; Dox: oxidized electron donor; hν: incident photon; ETC: electron transport chain.
Fig. 2. Constructing reducing power regeneration module. (a) CLSM image illustrating the biosynthesis of CdSe nanoparticles in E. coli. (b) Cross-section TEM image illustrating the localization of CdSe nanoparticles in E. coli cells. c, HETEM image and lattice fringes of CdSe nanoparticles. (d?g) HAADF-STEM image of CdSe. (h?j) The mapping of EDS in E. coli JZ-CdSe. (k) ICP-MS illustrating the absorption of Cd2+ and SeO32? ions. (l) The spot scan of EDS in E. coli JZ-CdSe. (m) XPS analysis of CdSe nanoparticles. (n) Survival rate of E. coli JZ-CdSe cells.
Fig. 3. Evaluating reducing power regeneration module. (a) UV-vis DRS spectra of E. coli JZ-CdSe. (b) Bandgap width of CdSe QDs. (c) Transient photocurrent of E. coli JZ-CdSe. (d) Electrochemical impedance spectroscopy of E. coli JZ-CdSe. (e,f) The intracellular NADH contents of E. coli JZ-CdSe. (g) The absorbance of E. coli JZ-CdSe using electron acceptor methyl orange. (h) Evaluating the regenerated NADH for bioproduction in vivo. (i) Evaluating NADH regeneration for bioproduction in vitro.
Fig. 4. Developing LDBS by integrating the SM cycle and reducing power regeneration module. (a,b) LDBS was developed by assembling the SM cycle and reducing power regeneration module in vitro and in vivo. (c) Acetyl-CoA production with LDBS under light condition in vitro. (d) Acetyl-CoA production with LDBS in E. coli JZ-C2-CdSe under light condition in vivo. Sal, serine aldolase; Sda, serine deaminase; Me, malic enzyme; Mtk, malate thiokinase; Mcl, malyl-CoA lyase; Agt, aspartate-glyoxylate transaminase; e?, electron; Dred, reduced electron donor; Dox, oxidized electron donor; hν, incident photon, ETC, electron transport chain.
Fig. 5. Programming LDBS for C3-compounds and C4-compounds production. (a) The SM cycle in LDBS was extended for transforming acetyl-CoA into pyruvate by assembling SMP pathway and reducing power regeneration module. (b) Pyruvate production with E. coli JZ-C3-CdSe under light condition in vivo. (c) The SM cycle in LDBS was extended for transforming acetyl-CoA into C4-compounds by assembling SMAPS pathway and reducing power regeneration module. (d) Succinate production with E. coli JZ-C4-CdSe under light condition in vivo. Adh, acetaldehyde dehydrogenase; Pdc, pyruvate decarboxylase; Acc, acetyl-CoA carboxylase; Mcr, malonyl-CoA reductase; Pcs, multifunctional propionyl-CoA synthetase; Pcc, propionyl-CoA carboxylase; Epi, methylmalonyl-CoA epimerase; Mcm, methylmalonyl-CoA mutase; Smt, succinyl-CoA: L-malate CoA-transferase; e-, electron; Dred, reduced electron donor; Dox, oxidized electron donor; hν, incident photon, ETC, electron transport chain.
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