Enzymatic C1 reduction using hydrogen in cofactor regeneration
Received date: 13 Dec 2023
Accepted date: 16 Feb 2024
Copyright
Carbon dioxide fixation presents a potential solution for mitigating the greenhouse gas issue. During carbon dioxide fixation, C1 compound reduction requires a high energy supply. Thermodynamic calculations suggest that the energy source for cofactor regeneration plays a vital role in the effective enzymatic C1 reduction. Hydrogenase utilizes renewable hydrogen to achieve the regeneration and supply cofactor nicotinamide adenine dinucleotide (NADH), providing a driving force for the reduction reaction to reduce the thermodynamic barrier of the reaction cascade, and making the forward reduction pathway thermodynamically feasible. Based on the regeneration of cofactor NADH by hydrogenase, and coupled with formaldehyde dehydrogenase and formolase, a favorable thermodynamic mode of the C1 reduction pathway for reducing formate to dihydroxyacetone (DHA) was designed and constructed. This resulted in accumulation of 373.19 μmol·L–1 DHA after 2 h, and conversion reaching 7.47%. These results indicate that enzymatic utilization of hydrogen as the electron donor to regenerate NADH is of great significance to the sustainable and green development of bio-manufacturing because of its high economic efficiency, no by-products, and environment-friendly operation. Moreover, formolase efficiently and selectively fixed the intermediate formaldehyde (FALD) to DHA, thermodynamically pulled formate to efficiently reduce to DHA, and finally stored the low-grade renewable energy into chemical energy with high energy density.
Ruishuang Sun , Chenqi Cao , Qingyun Wang , Hui Cao , Ulrich Schwaneberg , Yu Ji , Luo Liu , Haijun Xu . Enzymatic C1 reduction using hydrogen in cofactor regeneration[J]. Frontiers of Chemical Science and Engineering, 2024 , 18(7) : 75 . DOI: 10.1007/s11705-024-2431-3
1 |
Zhang C , Ottenheim C , Weingarten M , Ji L H . Microbial utilization of next-generation feedstocks for the biomanufacturing of value-added chemicals and food ingredients. Frontiers in Bioengineering and Biotechnology, 2022, 10: 874612
|
2 |
Artz J , Müller T E , Thenert K , Kleinekorte J , Meys R , Sternberg A , Bardow A , Leitner W . Sustainable conversion of carbon dioxide: an integrated review of catalysis and life cycle assessment. Chemical Reviews, 2018, 118(2): 434–504
|
3 |
Yishai O , Lindner S N , de la Cruz J G , Tenenboim H , Bar-Even A . The formate bio-economy. Current Opinion in Chemical Biology, 2016, 35: 1–9
|
4 |
Hu Z C , Zheng Y G , Shen Y C . Dissolved-oxygen-stat fed-batch fermentation of 1,3-dihydroxyacetone from glycerol by Gluconobacter oxydans ZJB09112. Biotechnology and Bioprocess Engineering, 2010, 15(4): 651–656
|
5 |
Wu H , Tian C Y , Song X K , Liu C , Yang D , Jiang Z Y . Methods for the regeneration of nicotinamide coenzymes. Green Chemistry, 2013, 15(7): 1773–1789
|
6 |
Lee Y S , Gerulskis R , Minteer S D . Advances in electrochemical cofactor regeneration: enzymatic and non-enzymatic approaches. Current Opinion in Biotechnology, 2022, 73: 14–21
|
7 |
Sharma V K , Hutchison J M , Allgeier A M . Redox biocatalysis: quantitative comparisons of nicotinamide cofactor regeneration methods. ChemSusChem, 2022, 15(22): e202200888
|
8 |
Lee S H , Choi D S , Kuk S K , Park C B . Photobiocatalysis: activating redox enzymes by direct or indirect transfer of photoinduced electrons. Angewandte Chemie International Edition, 2018, 57(27): 7958–7985
|
9 |
Wang X , Saba T , Yiu H H P , Howe R F , Anderson J A , Shi J . Cofactor NAD(P)H regeneration inspired by heterogeneous pathways. Chem, 2017, 2(5): 621–654
|
10 |
Calvin S J , Mangan D , Miskelly I , Moody T S , Stevenson P J . Overcoming equilibrium issues with carbonyl reductase enzymes. Organic Process Research & Development, 2012, 16(1): 82–86
|
11 |
Hollmann F , Arends I W C E , Holtmann D . Enzymatic reductions for the chemist. Green Chemistry, 2011, 13(9): 2285–2313
|
12 |
Schiffels J , Pinkenburg O , Schelden M , Aboulnaga E A A , Baumann M E M , Selmer T . An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant NiFe-hydrogenase from Cupriavidus necator in Escherichia coli. PLoS One, 2013, 8(7): e68812
|
13 |
Siegel J B , Smith A L , Poust S , Wargacki A J , Bar-Even A , Louw C , Shen B W , Eiben C B , Tran H M , Noor E .
|
14 |
Friedrich B , Fritsch J , Lenz O . Oxygen-tolerant hydrogenases in hydrogen-based technologies. Current Opinion in Biotechnology, 2011, 22(3): 358–364
|
15 |
Kim K J , Kim H E , Lee K H , Han W , Yi M J , Jeong J , Oh B H . Two-promoter vector is highly efficient for overproduction of protein complexes. Protein Science, 2004, 13(6): 1698–1703
|
16 |
Studier F W . Protein production by auto-induction in high density shaking cultures. Protein Expression and Purification, 2005, 41(1): 207–234
|
17 |
Schiffels J , Selmer T . A flexible toolbox to study protein-assisted metalloenzyme assembly in vitro. Biotechnology and Bioengineering, 2015, 112(11): 2360–2372
|
18 |
Schütte H , Flossdorf J , Sahm H , Kula M R . Purification and properties of formaldehyde dehydrogenase and formate dehydrogenase from Candida boidinii. European Journal of Biochemistry, 1976, 62(1): 151–160
|
19 |
Khana D B , Callaghan M M , Amador-Noguez D . Novel computational and experimental approaches for investigating the thermodynamics of metabolic networks. Current Opinion in Microbiology, 2022, 66: 21–31
|
20 |
Alberty R A . Thermodynamics of systems of biochemical reactions. Journal of Theoretical Biology, 2002, 215(4): 491–501
|
21 |
Zhao T , Li Y , Zhang Y . Biological carbon fixation: a thermodynamic perspective. Green Chemistry, 2021, 23(20): 7852–7864
|
22 |
Flamholz A , Noor E , Bar-Even A , Milo R . eQuilibrator-the biochemical thermodynamics calculator. Nucleic Acids Research, 2012, 40(D1): D770–D775
|
23 |
Lonsdale T H , Lauterbach L , Malca S H , Nestl B M , Hauer B , Lenz O . H2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O2-tolerant hydrogenase and a P450 monooxygenase. Chemical Communications, 2015, 51(90): 16173–16175
|
24 |
Lv X , Yu W , Zhang C , Ning P , Li J , Liu Y , Du G , Liu L . C1-based biomanufacturing: advances, challenges and perspectives. Bioresource Technology, 2023, 367: 128259
|
25 |
Yishai O , Bouzon M , Doring V , Bar-Even A . In vivo assimilation of one-carbon via a synthetic reductive glycine pathway in Escherichia coli. ACS Synthetic Biology, 2018, 7(9): 2023–2028
|
26 |
Sanchez-Moreno I , Garcia-Garcia J F , Bastida A , Garcia-Junceda E . Multienzyme system for dihydroxyacetone phosphate-dependent aldolase catalyzed C–C bond formation from dihydroxyacetone. Chemical Communications, 2004, (14): 1634–1635
|
27 |
Katryniok B , Kimura H , Skrzynska E , Girardon J S , Fongarland P , Capron M , Ducoulombier R , Mimura N , Paul S , Dumeignil F . Selective catalytic oxidation of glycerol: perspectives for high value chemicals. Green Chemistry, 2011, 13(8): 1960–1979
|
28 |
Cai T , Sun H , Qiao J , Zhu L , Zhang F , Zhang J , Tang Z , Wei X , Yang J , Yuan Q .
|
29 |
Salehizadeh H , Yan N , Farnood R . Recent advances in microbial CO2 fixation and conversion to value-added products. Chemical Engineering Journal, 2020, 390: 124584
|
30 |
Satanowski A , Bar-Even A . A one-carbon path for fixing CO2. EMBO Reports, 2020, 21(4): e50273
|
/
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