agents. In: Supuran CT, Nocentini A (eds) Carbonic Anhydrases. Academic Press, pp 449–
475. https://doi.org/10.1016/B978-0-12-816476-1.00020-4
17. Rowlett RS (2010) Structure and catalytic mechanism of the b-carbonic anhydrases.
Biochimica et Biophysica Acta (BBA) Proteins Proteomics 1804(2):362–373. https://doi.
org/10.1016/j.bbapap.2009.08.002
18. Boone CD, Habibzadegan A, Tu C, Silverman DN, McKenna R (2013) Structural and
catalytic characterization of a thermally stable and acid-stable variant of human carbonic
anhydrase II containing an engineered disulfide bond. Acta Crystallographica Sect D 69
(8):1414–1422. https://doi.org/10.1107/S0907444913008743
19. Díaz-Torres NA, Mahon BP, Boone CD, Pinard MA, Tu C, Ng R, Agbandje-McKenna M,
Silverman D, Scott K, McKenna R (2015) Structural and biophysical characterization of the
a-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2:
insights into engineering thermostable enzymes for CO2 sequestration. Acta Crystallogr D
Biol Crystallogr 71(Pt 8):1745–1756. https://doi.org/10.1107/s1399004715012183
20. Sundaram S, Thakur IS (2018) Induction of calcite precipitation through heightened
production of extracellular carbonic anhydrase by CO2 sequestering bacteria. Biores
Technol 253:368–371. https://doi.org/10.1016/j.biortech.2018.01.081
21. Lu WP, Ragsdale SW (1991) Reductive activation of the coenzyme A/acetyl-CoA isotopic
exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium
thermoaceticum and its inhibition by nitrous oxide and carbon monoxide. J Biol Chem
266(6):3554–3564
22. Burton R, Can M, Esckilsen D, Wiley S, Ragsdale SW (2018) Chapter twelve—production
and properties of enzymes that activate and produce carbon monoxide. In: Armstrong F
(ed) Methods in enzymology, vol 613. Academic Press, pp 297–324. https://doi.org/10.
1016/bs.mie.2018.10.005
23. Evans DJ (2005) Chemistry relating to the nickel enzymes CODH and ACS. Coord Chem
Rev 249(15):1582–1595. https://doi.org/10.1016/j.ccr.2004.09.012
24. Wang VCC, Ragsdale SW, Armstrong FA (2014) Investigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon
monoxide dehydrogenases. Metal Ions Life Sci 14:71–97. https://doi.org/10.1007/978-94017-9269-1_4
25. Ragsdale SW (2004) Life with carbon monoxide. Crit Rev Biochem Mol Biol 39(3):165–
195. https://doi.org/10.1080/10409230490496577
26. Cordas CM, Moura JJG (2019) Molybdenum and tungsten enzymes redox properties—a
brief overview. Coord Chem Rev 394:53–64. https://doi.org/10.1016/j.ccr.2019.05.005
27. Wang VCC, Ragsdale SW, Armstrong FA (2013) Investigations of two bidirectional carbon
monoxide dehydrogenases from carboxydothermus hydrogenoformans by protein film
electrochemistry. ChemBioChem 14(14):1845–1851. https://doi.org/10.1002/cbic.201300270
28. Wang VCC, Islam STA, Can M, Ragsdale SW, Armstrong FA (2015) Investigations by protein
film electrochemistry of alternative reactions of nickel-containing carbon monoxide dehydrogenase. J Phys Chem B 119(43):13690–13697. https://doi.org/10.1021/acs.jpcb.5b03098
29. Alfano M, Cavazza C (2018) The biologically mediated water–gas shift reaction: structure,
function and biosynthesis of monofunctional [NiFe]-carbon monoxide dehydrogenases.
Sustain Energy Fuels 2(8):1653–1670. https://doi.org/10.1039/c8se00085a
30. Maia LB, Fonseca L, Moura I, Moura JJG (2016) Reduction of carbon dioxide by a
molybdenum-containing formate dehydrogenase: a kinetic and mechanistic study. J Am
Chem Soc 138(28):8834–8846. https://doi.org/10.1021/jacs.6b03941
31. Niks D, Duvvuru J, Escalona M, Hille R (2016) Spectroscopic and kinetic properties of the
molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha. J Biol Chem 291(3):1162–1174
32. Bassegoda A, Madden C, Wakerley DW, Reisner E, Hirst J (2014) Reversible interconversion of CO 2 and formate by a molybdenum-containing formate dehydrogenase. J Am
Chem Soc 136(44):15473–15476. https://doi.org/10.1021/ja508647u
Carbon Dioxide Utilization—Bioelectrochemical Approaches
101
475. https://doi.org/10.1016/B978-0-12-816476-1.00020-4
17. Rowlett RS (2010) Structure and catalytic mechanism of the b-carbonic anhydrases.
Biochimica et Biophysica Acta (BBA) Proteins Proteomics 1804(2):362–373. https://doi.
org/10.1016/j.bbapap.2009.08.002
18. Boone CD, Habibzadegan A, Tu C, Silverman DN, McKenna R (2013) Structural and
catalytic characterization of a thermally stable and acid-stable variant of human carbonic
anhydrase II containing an engineered disulfide bond. Acta Crystallographica Sect D 69
(8):1414–1422. https://doi.org/10.1107/S0907444913008743
19. Díaz-Torres NA, Mahon BP, Boone CD, Pinard MA, Tu C, Ng R, Agbandje-McKenna M,
Silverman D, Scott K, McKenna R (2015) Structural and biophysical characterization of the
a-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2:
insights into engineering thermostable enzymes for CO2 sequestration. Acta Crystallogr D
Biol Crystallogr 71(Pt 8):1745–1756. https://doi.org/10.1107/s1399004715012183
20. Sundaram S, Thakur IS (2018) Induction of calcite precipitation through heightened
production of extracellular carbonic anhydrase by CO2 sequestering bacteria. Biores
Technol 253:368–371. https://doi.org/10.1016/j.biortech.2018.01.081
21. Lu WP, Ragsdale SW (1991) Reductive activation of the coenzyme A/acetyl-CoA isotopic
exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium
thermoaceticum and its inhibition by nitrous oxide and carbon monoxide. J Biol Chem
266(6):3554–3564
22. Burton R, Can M, Esckilsen D, Wiley S, Ragsdale SW (2018) Chapter twelve—production
and properties of enzymes that activate and produce carbon monoxide. In: Armstrong F
(ed) Methods in enzymology, vol 613. Academic Press, pp 297–324. https://doi.org/10.
1016/bs.mie.2018.10.005
23. Evans DJ (2005) Chemistry relating to the nickel enzymes CODH and ACS. Coord Chem
Rev 249(15):1582–1595. https://doi.org/10.1016/j.ccr.2004.09.012
24. Wang VCC, Ragsdale SW, Armstrong FA (2014) Investigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon
monoxide dehydrogenases. Metal Ions Life Sci 14:71–97. https://doi.org/10.1007/978-94017-9269-1_4
25. Ragsdale SW (2004) Life with carbon monoxide. Crit Rev Biochem Mol Biol 39(3):165–
195. https://doi.org/10.1080/10409230490496577
26. Cordas CM, Moura JJG (2019) Molybdenum and tungsten enzymes redox properties—a
brief overview. Coord Chem Rev 394:53–64. https://doi.org/10.1016/j.ccr.2019.05.005
27. Wang VCC, Ragsdale SW, Armstrong FA (2013) Investigations of two bidirectional carbon
monoxide dehydrogenases from carboxydothermus hydrogenoformans by protein film
electrochemistry. ChemBioChem 14(14):1845–1851. https://doi.org/10.1002/cbic.201300270
28. Wang VCC, Islam STA, Can M, Ragsdale SW, Armstrong FA (2015) Investigations by protein
film electrochemistry of alternative reactions of nickel-containing carbon monoxide dehydrogenase. J Phys Chem B 119(43):13690–13697. https://doi.org/10.1021/acs.jpcb.5b03098
29. Alfano M, Cavazza C (2018) The biologically mediated water–gas shift reaction: structure,
function and biosynthesis of monofunctional [NiFe]-carbon monoxide dehydrogenases.
Sustain Energy Fuels 2(8):1653–1670. https://doi.org/10.1039/c8se00085a
30. Maia LB, Fonseca L, Moura I, Moura JJG (2016) Reduction of carbon dioxide by a
molybdenum-containing formate dehydrogenase: a kinetic and mechanistic study. J Am
Chem Soc 138(28):8834–8846. https://doi.org/10.1021/jacs.6b03941
31. Niks D, Duvvuru J, Escalona M, Hille R (2016) Spectroscopic and kinetic properties of the
molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha. J Biol Chem 291(3):1162–1174
32. Bassegoda A, Madden C, Wakerley DW, Reisner E, Hirst J (2014) Reversible interconversion of CO 2 and formate by a molybdenum-containing formate dehydrogenase. J Am
Chem Soc 136(44):15473–15476. https://doi.org/10.1021/ja508647u
Carbon Dioxide Utilization—Bioelectrochemical Approaches
101