90. Cui W, Liu Q, Xing ZC, Asiri AM, Alamry KA, Sun X (2015) MoP nanosheets supported
on biomass-derived carbon flake: One-step facile preparation and application as a novel
high-active electrocatalyst toward hydrogen evolution reaction. Appl Catal B 164:144–150
91. Morozan A, Goellner V, Zitolo A, Fonda E, Donnadieu B, Jones D, Jaouen F (2015)
Synergy between molybdenum nitride and gold leading to platinum-like activity for
hydrogen evolution. Phys Chem Chem Phys 17:4047–4053
92. Darensbourg MY, Eduaran EL, Ding S, Lunsford AL, Pathirana KD, Ghosh P, Yang X
(2020) Hydrides, carbonyls, and metal—metal bonds: organometallic chemistry control of
hydrogenases. In: Moura JJG, Moura I, Maia L (eds) Enzymes for solving humankind’s
problems, Springer Nature Switzerland AG (in press)
93. Martins M, Pereira IAC, Pita M, De Lacey AL (2020) Biological production of hydrogen. In:
Moura JJG, Moura I, Maia L (eds) Enzymes for solving humankind’s problems, Springer
Nature Switzerland AG (in press)
94. Grimaldi S, Schoepp-Cothenet B, Ceccaldi P, Guigliarelli B, Magalon A (2013) The
prokaryotic Mo/W-bisPGD enzymes family: a catalytic workhorse in bioenergetic. Biochim
Biophys Acta 1827:1048–1085
95. Hartmann T, Schwanhold N, Leimkühler S (2015) Assembly and catalysis of molybdenum
or tungsten-containing formate dehydrogenases from bacteria. Biochim Biophys Acta
1854:1090–1100
96. Maia LB, Moura JJG, Moura I (2015) Molybdenum and tungsten-dependent formate
dehydrogenases. J Biol Inorg Chem 20:287–309
97. Magalon A, Ceccaldi P, Schoepp-Cothenet B (2017) The Prokaryotic Mo/W-bisPGD
Enzymes Family. In: Hille R, Schulzke C, Kirk M (eds) Molybdenum and tungsten
enzymes: biochemistry, RSC Metallobiology Series No. 5, The Royal Society of Chemistry,
Cambridge, Chap. 5, p 143–191
98. 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
99. Niks D, Hille R (2018) Reductive activation of CO 2 by formate dehydrogenases. Methods
Enzymol 613:277–295
100. Niks D, Hille R (2019) Molybdenum—and tungsten-containing formate dehydrogenases and
formylmethanofuran dehydrogenases: structure mechanism, and cofactor insertion. Ptot Sci
28:111–122
101. Nielsen CF, Lange L, Meyer AS (2019) Classification and enzyme kinetics of formate
dehydrogenases for biomanufacturing via CO 2 utilization. Biotechnol Adv 37:107408
102. Kato N (1990) Formate dehydrogenase from methylotrophic yeasts. Methods Enzymol
188:459–462
103. Vinals C, Depiereux E, Feytmans E (1993) Prediction of structurally conserved regions of
D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.
Biochem Biophys Res Commun 192:182–188
104. Popov VO, Lamzin VS (1994) NAD + -dependent formate dehydrogenase. Biochem J
301:625–643
105. Filippova EV, Polyakov KM, Tikhonova TV, Stekhanova TN, Boiko KM, Popov KO
(2005) Structure of a new crystal modification of the bacterial NAD-dependent formate
dehydrogenase with a resolution of 2.1 Å. Crystallogr Rep 50:796–800
106. Schirwitz K, Schmidt A, Lamzin VS (2007) High resolution structures of formate
dehydrogenase from Candida boidinii. Protein Sci 16:1146–1156
107. Shabalin IG, Polyakov KM, Tishkov VI, Popov VO (2009) Atomic resolution crystal
structure of NAD(+)-dependent formate dehydrogenase from bacterium moraxella Sp. C-1.
Acta Nat 1:89–93
108. Alekseeva AA, Savin SS, Tishkov VI (2011) NAD (+) -dependent formate dehydrogenase
from plants. Acta Nat 3:38–54
Carbon Dioxide Utilisation—The Formate Route
71
on biomass-derived carbon flake: One-step facile preparation and application as a novel
high-active electrocatalyst toward hydrogen evolution reaction. Appl Catal B 164:144–150
91. Morozan A, Goellner V, Zitolo A, Fonda E, Donnadieu B, Jones D, Jaouen F (2015)
Synergy between molybdenum nitride and gold leading to platinum-like activity for
hydrogen evolution. Phys Chem Chem Phys 17:4047–4053
92. Darensbourg MY, Eduaran EL, Ding S, Lunsford AL, Pathirana KD, Ghosh P, Yang X
(2020) Hydrides, carbonyls, and metal—metal bonds: organometallic chemistry control of
hydrogenases. In: Moura JJG, Moura I, Maia L (eds) Enzymes for solving humankind’s
problems, Springer Nature Switzerland AG (in press)
93. Martins M, Pereira IAC, Pita M, De Lacey AL (2020) Biological production of hydrogen. In:
Moura JJG, Moura I, Maia L (eds) Enzymes for solving humankind’s problems, Springer
Nature Switzerland AG (in press)
94. Grimaldi S, Schoepp-Cothenet B, Ceccaldi P, Guigliarelli B, Magalon A (2013) The
prokaryotic Mo/W-bisPGD enzymes family: a catalytic workhorse in bioenergetic. Biochim
Biophys Acta 1827:1048–1085
95. Hartmann T, Schwanhold N, Leimkühler S (2015) Assembly and catalysis of molybdenum
or tungsten-containing formate dehydrogenases from bacteria. Biochim Biophys Acta
1854:1090–1100
96. Maia LB, Moura JJG, Moura I (2015) Molybdenum and tungsten-dependent formate
dehydrogenases. J Biol Inorg Chem 20:287–309
97. Magalon A, Ceccaldi P, Schoepp-Cothenet B (2017) The Prokaryotic Mo/W-bisPGD
Enzymes Family. In: Hille R, Schulzke C, Kirk M (eds) Molybdenum and tungsten
enzymes: biochemistry, RSC Metallobiology Series No. 5, The Royal Society of Chemistry,
Cambridge, Chap. 5, p 143–191
98. 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
99. Niks D, Hille R (2018) Reductive activation of CO 2 by formate dehydrogenases. Methods
Enzymol 613:277–295
100. Niks D, Hille R (2019) Molybdenum—and tungsten-containing formate dehydrogenases and
formylmethanofuran dehydrogenases: structure mechanism, and cofactor insertion. Ptot Sci
28:111–122
101. Nielsen CF, Lange L, Meyer AS (2019) Classification and enzyme kinetics of formate
dehydrogenases for biomanufacturing via CO 2 utilization. Biotechnol Adv 37:107408
102. Kato N (1990) Formate dehydrogenase from methylotrophic yeasts. Methods Enzymol
188:459–462
103. Vinals C, Depiereux E, Feytmans E (1993) Prediction of structurally conserved regions of
D-specific hydroxy acid dehydrogenases by multiple alignment with formate dehydrogenase.
Biochem Biophys Res Commun 192:182–188
104. Popov VO, Lamzin VS (1994) NAD + -dependent formate dehydrogenase. Biochem J
301:625–643
105. Filippova EV, Polyakov KM, Tikhonova TV, Stekhanova TN, Boiko KM, Popov KO
(2005) Structure of a new crystal modification of the bacterial NAD-dependent formate
dehydrogenase with a resolution of 2.1 Å. Crystallogr Rep 50:796–800
106. Schirwitz K, Schmidt A, Lamzin VS (2007) High resolution structures of formate
dehydrogenase from Candida boidinii. Protein Sci 16:1146–1156
107. Shabalin IG, Polyakov KM, Tishkov VI, Popov VO (2009) Atomic resolution crystal
structure of NAD(+)-dependent formate dehydrogenase from bacterium moraxella Sp. C-1.
Acta Nat 1:89–93
108. Alekseeva AA, Savin SS, Tishkov VI (2011) NAD (+) -dependent formate dehydrogenase
from plants. Acta Nat 3:38–54
Carbon Dioxide Utilisation—The Formate Route
71