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https://doi.org/10.1039/c8ee01419a
137. Prévoteau A, Carvajal-Arroyo JM, Ganigué R, Rabaey K (2020) Microbial electrosynthesis
from CO 2 : forever a promise? Curr Opin Biotechnol 62:48–57. https://doi.org/10.1016/j.
copbio.2019.08.014
138. Bajracharya S, van den Burg B, Vanbroekhoven K, De Wever H, Buisman CJN, Pant D,
Strik DPBTB (2017) In situ acetate separation in microbial electrosynthesis from CO 2 using
ion-exchange resin. Electrochim Acta 237:267–275. https://doi.org/10.1016/j.electacta.2017.03.209
139. Bajracharya S, Vanbroekhoven K, De Wever H, Strik D, Buisman C, Pant D (2016)
integrated product separation in bioelectrochemical CO 2 reduction for improved process
efficiency. Chem Ing Tec 88(9):1255–1256. https://doi.org/10.1002/cite.201650202
140. Gutte B, Klauser S (2019) Design of catalytic polypeptides and proteins. Protein Eng Des
Sel 31(12):457–470. https://doi.org/10.1093/protein/gzz009
141. Laureanti JA, Ginovska B, Buchko GW, Schenter GK, Hebert M, Zadvornyy OA,
Peters JW, Shaw WJ (2020) A positive charge in the outer coordination sphere of an artificial
enzyme increases CO 2 hydrogenation. Organometallics 39(9):1532–1544. https://doi.org/10.
1021/acs.organomet.9b00843
142. Najafpour MM, Madadkhani S, Zand Z, Hołyńska M, Allakhverdiev SI (2016) Engineered
polypeptide around nano-sized manganese–calcium oxide as an artificial water-oxidizing enzyme
mimicking natural photosynthesis: toward artificial enzymes with highly active site densities. Int J
Hydrogen Energy 41(40):17826–17836. https://doi.org/10.1016/j.ijhydene.2016.07.024
143. Çakar MM, Ruupunen J, Mangas-Sanchez J, Birmingham WR, Yildirim D, Turunen O,
Turner NJ, Valjakka J, Binay B (2020) Engineered formate dehydrogenase from
chaetomium thermophilum, a promising enzymatic solution for biotechnical CO 2 fixation.
Biotech Lett. https://doi.org/10.1007/s10529-020-02937-7
144. Zhao H-Z, Chang Y-Y, Liu C (2013) Electrodes modified with iron porphyrin and carbon
nanotubes: application to CO 2 reduction and mechanism of synergistic electrocatalysis.
J Solid State Electrochem 17(6):1657–1664. https://doi.org/10.1007/s10008-013-2027-1
145. Martin LL, West LC, Wu B (2001) An extrusion strategy for the FeMo cofactor from
nitrogenase. Eur J Biochem 268(22):5676–5686. https://doi.org/10.1046/j.0014-2956.2001.
02506.x
146. Maiti BK, Maia LB, Silveira CM, Todorovic S, Carreira C, Carepo MSP, Grazina R,
Moura I, Pauleta SR, Moura JJG (2015) Incorporation of molybdenum in rubredoxin:
models for mononuclear molybdenum enzymes. J Biol Inorg Chem 20(5):821–829. https://
doi.org/10.1007/s00775-015-1268-0
147. Schlager S, Haberbauer M, Fuchsbauer A, Hemmelmair C, Dumitru LM, Hinterberger G,
Neugebauer H, Sariciftci NS (2017) Bio-electrocatalytic application of microorganisms for
carbon dioxide reduction to methane. Chemsuschem 10(1):226–233. https://doi.org/10.1002/
cssc.201600963
148. LaBelle EV, Marshall CW, May HD (2020) Microbiome for the electrosynthesis of
chemicals from carbon dioxide. Acc Chem Res 53(1):62–71. https://doi.org/10.1021/acs.
accounts.9b00522
149. Wu Z, Wang J, Liu J, Wang Y, Bi C, Zhang X (2019) Engineering an electroactive
Escherichia coli for the microbial electrosynthesis of succinate from glucose and CO 2 .
Microb Cell Fact 18(1):15. https://doi.org/10.1186/s12934-019-1067-3
150. Glaven SM (2019) Bioelectrochemical systems and synthetic biology: more power, more
products. Microb Biotechnol 12(5):819–823. https://doi.org/10.1111/1751-7915.13456
108
C. M. Cordas et al.