51. Tominaga J, Takahashi S, Sakamoto A, Shimada H (2020) Arabidopsis BSD2 reveals a
novel redox regulation of Rubisco physiology in vivo. Plant Signaling Behavior 15
(4):1740873. https://doi.org/10.1080/15592324.2020.1740873
52. Satagopan S, Sun Y, Parquette JR, Tabita FR (2017) Synthetic CO(2)-fixation enzyme
cascades immobilized on self-assembled nanostructures that enhance CO(2)/O(2) selectivity
of RubisCO. Biotechnol Biofuels 10:175–175. https://doi.org/10.1186/s13068-017-0861-6
53. Bhattacharya S, Schiavone M, Chakrabarti S, Bhattacharya SK (2003) CO 2 hydration by
immobilized carbonic anhydrase. Biotechnol Appl Biochem 38(2):111–117. https://doi.org/
10.1042/ba20030060
54. Zhu Y, Li W, Sun G, Tang Q, Bian H (2016) Enzymatic properties of immobilized carbonic
anhydrase and the biocatalyst for promoting CO2 capture in vertical reactor. Int J
Greenhouse Gas Control 49:290–296. https://doi.org/10.1016/j.ijggc.2016.03.016
55. Wanjari S, Prabhu C, Yadav R, Satyanarayana T, Labhsetwar N, Rayalu S (2011)
Immobilization of carbonic anhydrase on chitosan beads for enhanced carbonation reaction.
Process Biochem 46(4):1010–1018. https://doi.org/10.1016/j.procbio.2011.01.023
56. Hwang ET, Seo B-K, Gu MB, Zeng A-P (2016) Successful bi-enzyme stabilization for the
biomimetic cascade transformation of carbon dioxide. Catal Sci Technol 6(19):7267–7272.
https://doi.org/10.1039/c6cy00783j
57. Srikanth S, Alvarez-Gallego Y, Vanbroekhoven K, Pant D (2017) Enzymatic electrosynthesis of formic acid through carbon dioxide reduction in a bioelectrochemical system: effect
of immobilization and carbonic anhydrase addition. ChemPhysChem 18(22):3174–3181.
https://doi.org/10.1002/cphc.201700017
58. Addo PK, Arechederra RL, Waheed A, Shoemaker JD, Sly WS, Minteer SD (2011)
Methanol production via bioelectrocatalytic reduction of carbon dioxide: role of carbonic
anhydrase in improving electrode performance. Electrochem Solid-State Lett 14(4):E9–E13
59. Shin W, Lee SH, Shin JW, Lee SP, Kim Y (2003) Highly selective electrocatalytic conversion
of CO 2 to CO at −0.57 V (NHE) by carbon monoxide dehydrogenase from Moorella
thermoacetica. J Am Chem Soc 125(48):14688–14689. https://doi.org/10.1021/ja037370i
60. Reginald SS, Lee H, Lee YS, Yasin M, Chang IS (2020) Dissolved carbon monoxide
concentration monitoring platform based on direct electrical connection of CO dehydrogenase with electrically accessible surface structure. Biores Technol 297:122436. https://doi.
org/10.1016/j.biortech.2019.122436
61. Hwang HW, Yoon J, Min K, Kim M-S, Kim S-J, Cho DH, Susila H, Na J-G, Oh M-K,
Kim YH (2020) Two-stage bioconversion of carbon monoxide to biopolymers via formate as
an intermediate. Chem Eng J 389:124394. https://doi.org/10.1016/j.cej.2020.124394
62. Cordas CM, Campaniço M, Baptista R, Maia LB, Moura I, Moura JJG (2019) Direct
electrochemical reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase. J Inorg Biochem 196:110694. https://doi.org/10.1016/j.jinorgbio.2019.110694
63. Reda T, Plugge CM, Abram NJ, Hirst J (2008) Reversible interconversion of carbon dioxide
and formate by an electroactive enzyme. Proc Natl Acad Sci 105(31):10654
64. Sakai K, Sugimoto Y, Kitazumi Y, Shirai O, Takagi K, Kano K (2017) Direct electron
transfer-type bioelectrocatalytic interconversion of carbon dioxide/formate and NAD+/
NADH redox couples with tungsten-containing formate dehydrogenase. Electrochim Acta
228:537–544. https://doi.org/10.1016/j.electacta.2017.01.112
65. Sakai K, Kitazumi Y, Shirai O, Takagi K, Kano K (2017) Direct electron transfer-type
four-way bioelectrocatalysis of CO 2 /formate and NAD+/NADH redox couples by
tungsten-containing formate dehydrogenase adsorbed on gold nanoparticle-embedded
mesoporous carbon electrodes modified with 4-mercaptopyridine. Electrochem Commun
84:75–79. https://doi.org/10.1016/j.elecom.2017.10.005
66. Nielsen CF, Lange L, Meyer AS (2019) Classification and enzyme kinetics of formate
dehydrogenases for biomanufacturing via CO 2 utilization. Biotechnol Adv 37(7):107408.
https://doi.org/10.1016/j.biotechadv.2019.06.007
Carbon Dioxide Utilization—Bioelectrochemical Approaches
103
novel redox regulation of Rubisco physiology in vivo. Plant Signaling Behavior 15
(4):1740873. https://doi.org/10.1080/15592324.2020.1740873
52. Satagopan S, Sun Y, Parquette JR, Tabita FR (2017) Synthetic CO(2)-fixation enzyme
cascades immobilized on self-assembled nanostructures that enhance CO(2)/O(2) selectivity
of RubisCO. Biotechnol Biofuels 10:175–175. https://doi.org/10.1186/s13068-017-0861-6
53. Bhattacharya S, Schiavone M, Chakrabarti S, Bhattacharya SK (2003) CO 2 hydration by
immobilized carbonic anhydrase. Biotechnol Appl Biochem 38(2):111–117. https://doi.org/
10.1042/ba20030060
54. Zhu Y, Li W, Sun G, Tang Q, Bian H (2016) Enzymatic properties of immobilized carbonic
anhydrase and the biocatalyst for promoting CO2 capture in vertical reactor. Int J
Greenhouse Gas Control 49:290–296. https://doi.org/10.1016/j.ijggc.2016.03.016
55. Wanjari S, Prabhu C, Yadav R, Satyanarayana T, Labhsetwar N, Rayalu S (2011)
Immobilization of carbonic anhydrase on chitosan beads for enhanced carbonation reaction.
Process Biochem 46(4):1010–1018. https://doi.org/10.1016/j.procbio.2011.01.023
56. Hwang ET, Seo B-K, Gu MB, Zeng A-P (2016) Successful bi-enzyme stabilization for the
biomimetic cascade transformation of carbon dioxide. Catal Sci Technol 6(19):7267–7272.
https://doi.org/10.1039/c6cy00783j
57. Srikanth S, Alvarez-Gallego Y, Vanbroekhoven K, Pant D (2017) Enzymatic electrosynthesis of formic acid through carbon dioxide reduction in a bioelectrochemical system: effect
of immobilization and carbonic anhydrase addition. ChemPhysChem 18(22):3174–3181.
https://doi.org/10.1002/cphc.201700017
58. Addo PK, Arechederra RL, Waheed A, Shoemaker JD, Sly WS, Minteer SD (2011)
Methanol production via bioelectrocatalytic reduction of carbon dioxide: role of carbonic
anhydrase in improving electrode performance. Electrochem Solid-State Lett 14(4):E9–E13
59. Shin W, Lee SH, Shin JW, Lee SP, Kim Y (2003) Highly selective electrocatalytic conversion
of CO 2 to CO at −0.57 V (NHE) by carbon monoxide dehydrogenase from Moorella
thermoacetica. J Am Chem Soc 125(48):14688–14689. https://doi.org/10.1021/ja037370i
60. Reginald SS, Lee H, Lee YS, Yasin M, Chang IS (2020) Dissolved carbon monoxide
concentration monitoring platform based on direct electrical connection of CO dehydrogenase with electrically accessible surface structure. Biores Technol 297:122436. https://doi.
org/10.1016/j.biortech.2019.122436
61. Hwang HW, Yoon J, Min K, Kim M-S, Kim S-J, Cho DH, Susila H, Na J-G, Oh M-K,
Kim YH (2020) Two-stage bioconversion of carbon monoxide to biopolymers via formate as
an intermediate. Chem Eng J 389:124394. https://doi.org/10.1016/j.cej.2020.124394
62. Cordas CM, Campaniço M, Baptista R, Maia LB, Moura I, Moura JJG (2019) Direct
electrochemical reduction of carbon dioxide by a molybdenum-containing formate dehydrogenase. J Inorg Biochem 196:110694. https://doi.org/10.1016/j.jinorgbio.2019.110694
63. Reda T, Plugge CM, Abram NJ, Hirst J (2008) Reversible interconversion of carbon dioxide
and formate by an electroactive enzyme. Proc Natl Acad Sci 105(31):10654
64. Sakai K, Sugimoto Y, Kitazumi Y, Shirai O, Takagi K, Kano K (2017) Direct electron
transfer-type bioelectrocatalytic interconversion of carbon dioxide/formate and NAD+/
NADH redox couples with tungsten-containing formate dehydrogenase. Electrochim Acta
228:537–544. https://doi.org/10.1016/j.electacta.2017.01.112
65. Sakai K, Kitazumi Y, Shirai O, Takagi K, Kano K (2017) Direct electron transfer-type
four-way bioelectrocatalysis of CO 2 /formate and NAD+/NADH redox couples by
tungsten-containing formate dehydrogenase adsorbed on gold nanoparticle-embedded
mesoporous carbon electrodes modified with 4-mercaptopyridine. Electrochem Commun
84:75–79. https://doi.org/10.1016/j.elecom.2017.10.005
66. Nielsen CF, Lange L, Meyer AS (2019) Classification and enzyme kinetics of formate
dehydrogenases for biomanufacturing via CO 2 utilization. Biotechnol Adv 37(7):107408.
https://doi.org/10.1016/j.biotechadv.2019.06.007
Carbon Dioxide Utilization—Bioelectrochemical Approaches
103