33. Hille R, Hall J, Basu P (2014) The mononuclear molybdenum enzymes. Chem Rev 114
(7):3963–4038. https://doi.org/10.1021/cr400443z
34. Maia LB, Moura I, Moura JJG (2017) Molybdenum and tungsten-containing formate
dehydrogenases: aiming to inspire a catalyst for carbon dioxide utilization. Inorg Chim Acta
455:350–363. https://doi.org/10.1016/j.ica.2016.07.010
35. Amao Y (2018) Formate dehydrogenase for CO 2 utilization and its application. J CO 2 Util
26:623–641. https://doi.org/10.1016/j.jcou.2018.06.022
36. Maia LB, Moura I, Moura JJG (2017) Chapter 1 molybdenum and tungsten-containing
enzymes: an overview. In: Molybdenum and Tungsten Enzymes: Biochemistry. The Royal
Society of Chemistry, pp 1–80. https://doi.org/10.1039/9781782623915-00001
37. Zhang L, Liu J, Ong J, Li SFY (2016) Specific and sustainable bioelectro-reduction of
carbon dioxide to formate on a novel enzymatic cathode. Chemosphere 162:228–234.
https://doi.org/10.1016/j.chemosphere.2016.07.102
38. Zanello P (2019) Structure and electrochemistry of proteins harboring iron-sulfur clusters of
different nuclearities Part V. Nitrogenases. Coord Chem Rev 398:113004. https://doi.org/10.
1016/j.ccr.2019.07.001
39. Vicente EJ, Dean DR (2017) Keeping the nitrogen-fixation dream alive. Proc Natl Acad Sci
114(12):3009. https://doi.org/10.1073/pnas.1701560114
40. Seefeldt LC, Peters JW, Beratan DN, Bothner B, Minteer SD, Raugei S, Hoffman BM
(2018) Control of electron transfer in nitrogenase. Curr Opin Chem Biol 47:54–59. https://
doi.org/10.1016/j.cbpa.2018.08.011
41. Seefeldt LC, Yang Z-Y, Duval S, Dean DR (2013) Nitrogenase reduction of
carbon-containing compounds. Biochimica et Biophysica Acta (BBA) Bioenergetics 1827
(8):1102–1111. https://doi.org/10.1016/j.bbabio.2013.04.003
42. Newton WE, Dilworth MJ (2011) Assays of nitrogenase reaction products. In: Ribbe MW
(ed) Nitrogen fixation: methods and protocols. Humana Press, Totowa, NJ, pp 105–127.
https://doi.org/10.1007/978-1-61779-194-9_8
43. Seefeldt LC, Rasche ME, Ensign SA (1995) Carbonyl sulfide and carbon dioxide as new
substrates, and carbon disulfide as a new inhibitor, of nitrogenase. Biochemistry 34
(16):5382–5389. https://doi.org/10.1021/bi00016a009
44. Khadka N, Dean DR, Smith D, Hoffman BM, Raugei S, Seefeldt LC (2016) CO 2 reduction
catalyzed by nitrogenase: pathways to formate, carbon monoxide, and methane. Inorg Chem
55(17):8321–8330. https://doi.org/10.1021/acs.inorgchem.6b00388
45. Sugimura K, Kuwabata S, Yoneyama H (1990) Electrochemical fixation of carbon dioxide
in pyruvic acid to yield malic acid using malic enzyme as an electrocatalyst. Bioelectrochem
Bioenerg 24(2):241–247. https://doi.org/10.1016/0302-4598(90)85025-D
46. Zheng H, Ohno Y, Nakamori T, Suye S-i (2009) Production of l-malic acid with fixation of
HCO3− by malic enzyme-catalyzed reaction based on regeneration of coenzyme on
electrode modified by layer-by-layer self-assembly method. J Biosci Bioeng 107(1):16–20.
https://doi.org/10.1016/j.jbiosc.2008.09.009
47. Sugimura K, Kuwabata S, Yoneyama H (1989) Electrochemical fixation of carbon dioxide
in oxoglutaric acid using an enzyme as an electrocatalyst. J Am Chem Soc 111(6):2361–
2362. https://doi.org/10.1021/ja00188a093
48. García-Ferris C, Moreno J (1993) Redox regulation of enzymatic activity and proteolytic
susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase from Euglena gracilis.
Photosynth Res 35(1):55–66. https://doi.org/10.1007/bf02185411
49. Moreno J, García-Murria MJ, Marín-Navarro J (2008) Redox modulation of RubisCO
conformation and activity through its cysteine residues. J Exp Bot 59(7):1605–1614. https://
doi.org/10.1093/jxb/erm310
50. García-Murria MJ, Sudhani HPK, Marín-Navarro J, Sánchez del Pino MM, Moreno J (2018)
Dissecting the individual contribution of conserved cysteines to the redox regulation of
RubisCO. Photosynth Res 137(2):251–262. https://doi.org/10.1007/s11120-018-0497-9
102
C. M. Cordas et al.
(7):3963–4038. https://doi.org/10.1021/cr400443z
34. Maia LB, Moura I, Moura JJG (2017) Molybdenum and tungsten-containing formate
dehydrogenases: aiming to inspire a catalyst for carbon dioxide utilization. Inorg Chim Acta
455:350–363. https://doi.org/10.1016/j.ica.2016.07.010
35. Amao Y (2018) Formate dehydrogenase for CO 2 utilization and its application. J CO 2 Util
26:623–641. https://doi.org/10.1016/j.jcou.2018.06.022
36. Maia LB, Moura I, Moura JJG (2017) Chapter 1 molybdenum and tungsten-containing
enzymes: an overview. In: Molybdenum and Tungsten Enzymes: Biochemistry. The Royal
Society of Chemistry, pp 1–80. https://doi.org/10.1039/9781782623915-00001
37. Zhang L, Liu J, Ong J, Li SFY (2016) Specific and sustainable bioelectro-reduction of
carbon dioxide to formate on a novel enzymatic cathode. Chemosphere 162:228–234.
https://doi.org/10.1016/j.chemosphere.2016.07.102
38. Zanello P (2019) Structure and electrochemistry of proteins harboring iron-sulfur clusters of
different nuclearities Part V. Nitrogenases. Coord Chem Rev 398:113004. https://doi.org/10.
1016/j.ccr.2019.07.001
39. Vicente EJ, Dean DR (2017) Keeping the nitrogen-fixation dream alive. Proc Natl Acad Sci
114(12):3009. https://doi.org/10.1073/pnas.1701560114
40. Seefeldt LC, Peters JW, Beratan DN, Bothner B, Minteer SD, Raugei S, Hoffman BM
(2018) Control of electron transfer in nitrogenase. Curr Opin Chem Biol 47:54–59. https://
doi.org/10.1016/j.cbpa.2018.08.011
41. Seefeldt LC, Yang Z-Y, Duval S, Dean DR (2013) Nitrogenase reduction of
carbon-containing compounds. Biochimica et Biophysica Acta (BBA) Bioenergetics 1827
(8):1102–1111. https://doi.org/10.1016/j.bbabio.2013.04.003
42. Newton WE, Dilworth MJ (2011) Assays of nitrogenase reaction products. In: Ribbe MW
(ed) Nitrogen fixation: methods and protocols. Humana Press, Totowa, NJ, pp 105–127.
https://doi.org/10.1007/978-1-61779-194-9_8
43. Seefeldt LC, Rasche ME, Ensign SA (1995) Carbonyl sulfide and carbon dioxide as new
substrates, and carbon disulfide as a new inhibitor, of nitrogenase. Biochemistry 34
(16):5382–5389. https://doi.org/10.1021/bi00016a009
44. Khadka N, Dean DR, Smith D, Hoffman BM, Raugei S, Seefeldt LC (2016) CO 2 reduction
catalyzed by nitrogenase: pathways to formate, carbon monoxide, and methane. Inorg Chem
55(17):8321–8330. https://doi.org/10.1021/acs.inorgchem.6b00388
45. Sugimura K, Kuwabata S, Yoneyama H (1990) Electrochemical fixation of carbon dioxide
in pyruvic acid to yield malic acid using malic enzyme as an electrocatalyst. Bioelectrochem
Bioenerg 24(2):241–247. https://doi.org/10.1016/0302-4598(90)85025-D
46. Zheng H, Ohno Y, Nakamori T, Suye S-i (2009) Production of l-malic acid with fixation of
HCO3− by malic enzyme-catalyzed reaction based on regeneration of coenzyme on
electrode modified by layer-by-layer self-assembly method. J Biosci Bioeng 107(1):16–20.
https://doi.org/10.1016/j.jbiosc.2008.09.009
47. Sugimura K, Kuwabata S, Yoneyama H (1989) Electrochemical fixation of carbon dioxide
in oxoglutaric acid using an enzyme as an electrocatalyst. J Am Chem Soc 111(6):2361–
2362. https://doi.org/10.1021/ja00188a093
48. García-Ferris C, Moreno J (1993) Redox regulation of enzymatic activity and proteolytic
susceptibility of ribulose-1,5-bisphosphate carboxylase/oxygenase from Euglena gracilis.
Photosynth Res 35(1):55–66. https://doi.org/10.1007/bf02185411
49. Moreno J, García-Murria MJ, Marín-Navarro J (2008) Redox modulation of RubisCO
conformation and activity through its cysteine residues. J Exp Bot 59(7):1605–1614. https://
doi.org/10.1093/jxb/erm310
50. García-Murria MJ, Sudhani HPK, Marín-Navarro J, Sánchez del Pino MM, Moreno J (2018)
Dissecting the individual contribution of conserved cysteines to the redox regulation of
RubisCO. Photosynth Res 137(2):251–262. https://doi.org/10.1007/s11120-018-0497-9
102
C. M. Cordas et al.