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org/10.1021/acs.accounts.8b00551
68. Kuk SK, Gopinath K, Singh RK, Kim T-D, Lee Y, Choi WS, Lee J-K, Park CB (2019)
NADH-free electroenzymatic reduction of CO 2 by conductive hydrogel-conjugated formate
dehydrogenase. ACS Catalysis 9(6):5584–5589. https://doi.org/10.1021/acscatal.9b00127
69. Zhang L, Jiang Y, Jiang Z, Sun X, Shi J, Li L, Li J (2009) Biomimetic Fabrication of
hydroxyapatite–polysaccharide–formate dehydrogenase composite capsules for efficient
CO 2 conversion. J Biomater Sci Polym Ed 20(12):1661–1674. https://doi.org/10.1163/
156856208x386255
70. Watt GD, Burns A, Lough S, Tennent DL (1980) Redox and spectroscopic properties of
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71. Lydon BR, Lee CC, Tanifuji K, Sickerman NS, Newcomb MP, Hu Y, Ribbe MW, Yang JY
(2020) Electrochemical characterization of isolated nitrogenase cofactors from Azotobacter
vinelandii. ChemBioChem 21(12):1773–1778. https://doi.org/10.1002/cbic.201900425
72. Lee CC, Hu Y, Ribbe MW (2015) Catalytic reduction of CN−, CO, and CO 2 by nitrogenase
cofactors in lanthanide-driven reactions. Angew Chem Int Ed 54(4):1219–1222. https://doi.
org/10.1002/anie.201410412
73. Patel J, Cai R, Milton R, Chen H, Minteer SD (2020) Pyrene-based noncovalent
immobilization of nitrogenase on carbon surfaces. ChemBioChem 21(12):1729–1732.
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74. Hu B, Harris DF, Dean DR, Liu TL, Yang Z-Y, Seefeldt LC (2018) Electrocatalytic CO 2
reduction catalyzed by nitrogenase MoFe and FeFe proteins. Bioelectrochemistry 120:104–
109. https://doi.org/10.1016/j.bioelechem.2017.12.002
75. Sakai K, Kitazumi Y, Shirai O, Takagi K, Kano K (2016) Efficient bioelectrocatalytic CO 2
reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase. Electrochem Commun 73:85–88. https://doi.org/10.1016/j.elecom.2016.11.008
76. Sato R, Amao Y (2020) Can formate dehydrogenase from Candida boidinii catalytically
reduce carbon dioxide, bicarbonate, or carbonate to formate? New J Chem. https://doi.org/
10.1039/d0nj01183e
77. Ji C, Hou J, Wang K, Ng YH, Chen V (2017) Single-enzyme biofuel cells. Angew Chem Int
Ed 56(33):9762–9766. https://doi.org/10.1002/anie.201703980
78. Zhang L, Ong J, Liu J, Li SFY (2017) Enzymatic electrosynthesis of formate from CO 2
reduction in a hybrid biofuel cell system. Renew Energy 108:581–588. https://doi.org/10.
1016/j.renene.2017.03.009
79. Schoffelen S, van Hest JCM (2012) Multi-enzyme systems: bringing enzymes together
in vitro. Soft Matter 8(6):1736–1746. https://doi.org/10.1039/c1sm06452e
80. Kuwabata S, Tsuda R, Yoneyama H (1994) Electrochemical conversion of carbon dioxide to
methanol with the assistance of formate dehydrogenase and methanol dehydrogenase as
biocatalysts. J Am Chem Soc 116(12):5437–5443. https://doi.org/10.1021/ja00091a056
81. Ji X, Su Z, Ma G, Zhang S (2018) Sandwiching multiple dehydrogenases and shared
cofactor between double polyelectrolytes for enhanced communication of cofactor and
enzymes. Biochem Eng J 137:40–49. https://doi.org/10.1016/j.bej.2018.05.017
82. Carvalho RNL, Almeida RM, Moura JJG, Lourenço NT, Fonseca LJP, Cordas CM (2016)
Sandwich-type enzymatic fuel cell based on a new electro-conductive material—ion jelly.
ChemistrySelect 1(20):6546–6552. https://doi.org/10.1002/slct.201601640
83. Jiang Y, Su M, Zhang Y, Zhan G, Tao Y, Li D (2013) Bioelectrochemical systems for
simultaneously production of methane and acetate from carbon dioxide at relatively high rate.
Int J Hydrogen Energy 38(8):3497–3502. https://doi.org/10.1016/j.ijhydene.2012.12.107
104
C. M. Cordas et al.
electrochemically driven enzyme-catalyzed reduction of carbon dioxide to formate using
formate dehydrogenase and an artificial cofactor. Acc Chem Res 52(3):676–685. https://doi.
org/10.1021/acs.accounts.8b00551
68. Kuk SK, Gopinath K, Singh RK, Kim T-D, Lee Y, Choi WS, Lee J-K, Park CB (2019)
NADH-free electroenzymatic reduction of CO 2 by conductive hydrogel-conjugated formate
dehydrogenase. ACS Catalysis 9(6):5584–5589. https://doi.org/10.1021/acscatal.9b00127
69. Zhang L, Jiang Y, Jiang Z, Sun X, Shi J, Li L, Li J (2009) Biomimetic Fabrication of
hydroxyapatite–polysaccharide–formate dehydrogenase composite capsules for efficient
CO 2 conversion. J Biomater Sci Polym Ed 20(12):1661–1674. https://doi.org/10.1163/
156856208x386255
70. Watt GD, Burns A, Lough S, Tennent DL (1980) Redox and spectroscopic properties of
oxidized MoFe protein from Azotobacter vinelandii. Biochemistry 19(21):4926–4932.
https://doi.org/10.1021/bi00562a035
71. Lydon BR, Lee CC, Tanifuji K, Sickerman NS, Newcomb MP, Hu Y, Ribbe MW, Yang JY
(2020) Electrochemical characterization of isolated nitrogenase cofactors from Azotobacter
vinelandii. ChemBioChem 21(12):1773–1778. https://doi.org/10.1002/cbic.201900425
72. Lee CC, Hu Y, Ribbe MW (2015) Catalytic reduction of CN−, CO, and CO 2 by nitrogenase
cofactors in lanthanide-driven reactions. Angew Chem Int Ed 54(4):1219–1222. https://doi.
org/10.1002/anie.201410412
73. Patel J, Cai R, Milton R, Chen H, Minteer SD (2020) Pyrene-based noncovalent
immobilization of nitrogenase on carbon surfaces. ChemBioChem 21(12):1729–1732.
https://doi.org/10.1002/cbic.201900697
74. Hu B, Harris DF, Dean DR, Liu TL, Yang Z-Y, Seefeldt LC (2018) Electrocatalytic CO 2
reduction catalyzed by nitrogenase MoFe and FeFe proteins. Bioelectrochemistry 120:104–
109. https://doi.org/10.1016/j.bioelechem.2017.12.002
75. Sakai K, Kitazumi Y, Shirai O, Takagi K, Kano K (2016) Efficient bioelectrocatalytic CO 2
reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase. Electrochem Commun 73:85–88. https://doi.org/10.1016/j.elecom.2016.11.008
76. Sato R, Amao Y (2020) Can formate dehydrogenase from Candida boidinii catalytically
reduce carbon dioxide, bicarbonate, or carbonate to formate? New J Chem. https://doi.org/
10.1039/d0nj01183e
77. Ji C, Hou J, Wang K, Ng YH, Chen V (2017) Single-enzyme biofuel cells. Angew Chem Int
Ed 56(33):9762–9766. https://doi.org/10.1002/anie.201703980
78. Zhang L, Ong J, Liu J, Li SFY (2017) Enzymatic electrosynthesis of formate from CO 2
reduction in a hybrid biofuel cell system. Renew Energy 108:581–588. https://doi.org/10.
1016/j.renene.2017.03.009
79. Schoffelen S, van Hest JCM (2012) Multi-enzyme systems: bringing enzymes together
in vitro. Soft Matter 8(6):1736–1746. https://doi.org/10.1039/c1sm06452e
80. Kuwabata S, Tsuda R, Yoneyama H (1994) Electrochemical conversion of carbon dioxide to
methanol with the assistance of formate dehydrogenase and methanol dehydrogenase as
biocatalysts. J Am Chem Soc 116(12):5437–5443. https://doi.org/10.1021/ja00091a056
81. Ji X, Su Z, Ma G, Zhang S (2018) Sandwiching multiple dehydrogenases and shared
cofactor between double polyelectrolytes for enhanced communication of cofactor and
enzymes. Biochem Eng J 137:40–49. https://doi.org/10.1016/j.bej.2018.05.017
82. Carvalho RNL, Almeida RM, Moura JJG, Lourenço NT, Fonseca LJP, Cordas CM (2016)
Sandwich-type enzymatic fuel cell based on a new electro-conductive material—ion jelly.
ChemistrySelect 1(20):6546–6552. https://doi.org/10.1002/slct.201601640
83. Jiang Y, Su M, Zhang Y, Zhan G, Tao Y, Li D (2013) Bioelectrochemical systems for
simultaneously production of methane and acetate from carbon dioxide at relatively high rate.
Int J Hydrogen Energy 38(8):3497–3502. https://doi.org/10.1016/j.ijhydene.2012.12.107
104
C. M. Cordas et al.