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129. Silva SM, Pimentel C, Valente FMA, Rodrigues-Pousada C, Pereira IAC (2011) Tungsten
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130. Raaijmakers H, Macieira S, Dias JM, Texierira S, Bursakov S, Huber R, Moura JJG,
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Caldeira J, Moura JJ, Moura I (1999) Purification and characterization of a
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Romão MJ (2001) Tungsten-containing formate dehydrogenase from Desulfovibrio gigas:
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J Biol Inorg Chem 6:398–404
135. Costa C, Teixeira M, LeGall J, Moura JJG, Moura I (1997) Formate dehydrogenase from
Desulfovibrio desulfuricans ATCC 27774: isolation and spectroscopic characterization of
the active sites. J Biol Inorg Chem 2:198–208
136. Rivas M, Gonzalez P, Brondino CD, Moura JJG, Moura I (2007) EPR characterization of the
molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans ATCC
27774 upon formate reduction. J Inorg Biol 101:1617–1622
137. Maia L, 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 138:8834–8846
138. Young T, Niks D, Hakopian S, Tam TK, Yu X, Hille R, Blaha GM (2020) Crystallographic
and kinetic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase
FdsABG from Cupriavidus necator. J Biol Chem 295:6570–6585
139. Radon C, Mittelstädt G, Duffus BR, Bürger J, Hartmann T, Mielke T, Teutloff C,
Leimkühler S, Wendler P (2020) Cryo-EM structures reveal intricate Fe-S cluster
arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. Nat Commun
11:1912
140. Wagner T, Ermler U, Shima S (2016) The methanogenic CO2 reducing-and-fixing enzyme
is bifunctional and contains 46 [4Fe-4S] clusters. Science 354:114–117
141. Trchounian K, Poladyan A, Vassilian A, Trchounian A (2012) Multiple and reversible
hydrogenases for hydrogen production by Escherichia coli. Crit Rev Biochem Mol Biol
47:236–249
Carbon Dioxide Utilisation—The Formate Route
73
Ward N, Methe B, Brinkac LM, Daugherty SC, Deboy RT, Dodson RJ, Durkin AS,
Madupu R, Nelson WC, Sullivan SA, Fouts D, Haft DH, Selengut J, Peterson JD,
Davidsen TM, Zafar N, Zhou L, Radune D, Dimitrov G, Hance M, Tran K, Khouri H, Gill J,
Utterback TR, Feldblyum TV, Wall JD, Voordouw G, Fraser CM (2004) The genome
sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris hildenborough.
Nat Biotechnol 22:554–559
128. Mota CS, Valette O, Gonzalez PJ, Brondino CD, Moura JJG, Moura I, Dolla A, Rivas MG
(2011) Effects of molybdate and tungstate on expression levels and biochemical
characteristics of formate dehydrogenases produced by Desulfovibrio alaskensis NCIMB
13491. J Bacteriol 193:2917–2923
129. Silva SM, Pimentel C, Valente FMA, Rodrigues-Pousada C, Pereira IAC (2011) Tungsten
and molybdenum regulation of formate dehydrogenase expression in Desulfovibrio vulgaris
hildenborough. J Bacteriol 193:2908–2916
130. Raaijmakers H, Macieira S, Dias JM, Texierira S, Bursakov S, Huber R, Moura JJG,
Moura I, Romão MJ (2002) Gene sequence and the 18Å crystal structure of the
tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Structure 10:1261–
1272
131. da Silva SM, Voordouw J, Leitão C, Martins M, Voordouw G, Pereira IAC (2013) Function
of formate dehydrogenases in Desulfovibrio vulgaris hildenborough energy metabolism.
Microbiology 159:1760–1769
132. Oliveira AR, Mota C, Mourato C, Domingos RM, Santos MFA, Gesto D, Guigliarelli B,
Santos-Silva T, Romão MJ, Pereira IAC (2020) Toward the mechanistic understanding of
enzymatic CO 2 reduction. ACS Catal 10:3844–3856
133. Almendra MJ, Brondino CD, Gavel O, Pereira AS, Tavares P, Bursakov S, Duarte R,
Caldeira J, Moura JJ, Moura I (1999) Purification and characterization of a
tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Biochemistry
38:16366–16372
134. Raaijmakers H, Teixeira S, Dias JM, Almendra MJ, Brondino CD, Moura I, Moura JJ,
Romão MJ (2001) Tungsten-containing formate dehydrogenase from Desulfovibrio gigas:
metal identification and preliminary structural data by multi-wavelength crystallography.
J Biol Inorg Chem 6:398–404
135. Costa C, Teixeira M, LeGall J, Moura JJG, Moura I (1997) Formate dehydrogenase from
Desulfovibrio desulfuricans ATCC 27774: isolation and spectroscopic characterization of
the active sites. J Biol Inorg Chem 2:198–208
136. Rivas M, Gonzalez P, Brondino CD, Moura JJG, Moura I (2007) EPR characterization of the
molybdenum(V) forms of formate dehydrogenase from Desulfovibrio desulfuricans ATCC
27774 upon formate reduction. J Inorg Biol 101:1617–1622
137. Maia L, 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 138:8834–8846
138. Young T, Niks D, Hakopian S, Tam TK, Yu X, Hille R, Blaha GM (2020) Crystallographic
and kinetic analyses of the FdsBG subcomplex of the cytosolic formate dehydrogenase
FdsABG from Cupriavidus necator. J Biol Chem 295:6570–6585
139. Radon C, Mittelstädt G, Duffus BR, Bürger J, Hartmann T, Mielke T, Teutloff C,
Leimkühler S, Wendler P (2020) Cryo-EM structures reveal intricate Fe-S cluster
arrangement and charging in Rhodobacter capsulatus formate dehydrogenase. Nat Commun
11:1912
140. Wagner T, Ermler U, Shima S (2016) The methanogenic CO2 reducing-and-fixing enzyme
is bifunctional and contains 46 [4Fe-4S] clusters. Science 354:114–117
141. Trchounian K, Poladyan A, Vassilian A, Trchounian A (2012) Multiple and reversible
hydrogenases for hydrogen production by Escherichia coli. Crit Rev Biochem Mol Biol
47:236–249
Carbon Dioxide Utilisation—The Formate Route
73