109. Guo Q, Gakhar L, Wickersham K, Francis K, Vardi-Kilshtain A, Major DT, Cheatum CM,
Kohen A (2016) Structural and kinetic studies of formate dehydrogenase from candida
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110. Hille R, Hall J, Basu P (2014) The mononuclear molybdenum enzymes. Chem Rev
114:3963–4038
111. Maia L, Moura I, Moura JJG (2017) Molybdenum and tungsten-containing enzymes: an
overview. 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. 1, p 1–80
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10.1016/B978-0-12-409547-2.13932-0
113. Zinoni F, Birkmann A, Stadtman TC, Böck A (1986) Nucleotide sequence and expression of
the
selenocysteine-containing
polypeptide
of
formate
dehydrogenase
(Formate-Hydrogen-Lyase-Linked) from Escherichia coli. Proc Natl Acad Sci USA
83:4650–4654
114. Axley MJ, Grahame DA, Stadtman TC (1990) Escherichia coli formate-hydrogen Lyase.
J Biol Chem 265:18213–18218
115. Gladyshev VN, Boyington JC, Khangulov SV, Grahame DA, Stadtman TC, Sun PD (1996)
Characterization of crystalline formate dehydrogenase h from Escherichia coli. J Biol Chem
271:8095–8100
116. Boyington JC, Gladyshev VN, Khangulov SV, Stadtman T, Sun PD (1997) Crystal structure
of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine and an
Fe 4 S 4 cluster. Science 275:1305–1308
117. Raaijmakers HCA, Romão MJ (2006) Formate-reduced E coli formate dehydrogenase H: the
reinterpretation of the crystal structure suggests a new reaction mechanism. J Biol Inorg
Chem 11:849–854
118. Jormakka M, Tornroth S, Abramson J, Byrne B, Iwata S (2002) Purification and
crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli.
Acta Crystallogr D Biol Crystallogr 58:160–162
119. Jormakka M, Törnroth S, Byrne B, Iwata S (2002) Molecular basis of proton motive force
generation: structure of formate dehydrogenase-N. Science 2295:1863–1868
120. Wang H, Gunsalus RP (2003) Coordinate regulation of the Escherichia coli formate
dehydrogenase fdnGHI and fdhF genes in response to nitrate, nitrite and formate: roles fro
NarL and NarP. J Bacteriol 185:5076–5085
121. Pommier J, Mandrand MA, Holt SE, Boxer DH, Giodano G (1992) A second phenazine
methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli. Biochim
Biophys Acta 1107:305–313
122. Plunkett G, Burland V, Daniels DL, Blattner FR (1993) Analysis of the Escherichia coli
genome. Nucleic Acids Res 21:3391–3398
123. Abaibou H, Pommier J, Benoit JP, Giordano G, Mandrand M (1995) Expression and
characterization of the Escherichia coli fdo locus and a possible physiological role for
aerobic formate dehydrogenase. J Bacteriol 177:7141–7149
124. Bursakov S, Liu M-Y, Payne WJ, LeGall J, Moura I, Moura JJG (1995) Isolation and
preliminary characterization of a soluble nitrate reductase from the sulfate reducing organism
Desulfovibrio desulfuricans ATCC 27774. Anaerobe 1:55–60
125. Sebban C, Blanchard L, Bruschi M, Guerlesquin F (1995) Purification and characterization
of the formate dehydrogenase from Desulfovibrio vulgaris hildenborough. FEMS Microbiol
Lett 133:143–149
126. Brondino CD, Passeggi MCG, Caldeira J, Almendra MJ, Feio MJ, Moura JJG, Moura I
(2004) Incorporation of either molybdenum or tungsten into formate dehydrogenase from
Desulfovibrio alaskensis NCIMB 13491. J Biol Inorg Chem 9:145–151
72
L. B. Maia et al.
Kohen A (2016) Structural and kinetic studies of formate dehydrogenase from candida
boidinii. Biochemistry 55:2760–2771
110. Hille R, Hall J, Basu P (2014) The mononuclear molybdenum enzymes. Chem Rev
114:3963–4038
111. Maia L, Moura I, Moura JJG (2017) Molybdenum and tungsten-containing enzymes: an
overview. 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. 1, p 1–80
112. Maia L, Moura JJG (2018) Mononuclear molybdenum-containing enzymes. Reference
module in chemistry, molecular sciences and chemical engineering, pp 1–19. https://doi.org/
10.1016/B978-0-12-409547-2.13932-0
113. Zinoni F, Birkmann A, Stadtman TC, Böck A (1986) Nucleotide sequence and expression of
the
selenocysteine-containing
polypeptide
of
formate
dehydrogenase
(Formate-Hydrogen-Lyase-Linked) from Escherichia coli. Proc Natl Acad Sci USA
83:4650–4654
114. Axley MJ, Grahame DA, Stadtman TC (1990) Escherichia coli formate-hydrogen Lyase.
J Biol Chem 265:18213–18218
115. Gladyshev VN, Boyington JC, Khangulov SV, Grahame DA, Stadtman TC, Sun PD (1996)
Characterization of crystalline formate dehydrogenase h from Escherichia coli. J Biol Chem
271:8095–8100
116. Boyington JC, Gladyshev VN, Khangulov SV, Stadtman T, Sun PD (1997) Crystal structure
of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine and an
Fe 4 S 4 cluster. Science 275:1305–1308
117. Raaijmakers HCA, Romão MJ (2006) Formate-reduced E coli formate dehydrogenase H: the
reinterpretation of the crystal structure suggests a new reaction mechanism. J Biol Inorg
Chem 11:849–854
118. Jormakka M, Tornroth S, Abramson J, Byrne B, Iwata S (2002) Purification and
crystallization of the respiratory complex formate dehydrogenase-N from Escherichia coli.
Acta Crystallogr D Biol Crystallogr 58:160–162
119. Jormakka M, Törnroth S, Byrne B, Iwata S (2002) Molecular basis of proton motive force
generation: structure of formate dehydrogenase-N. Science 2295:1863–1868
120. Wang H, Gunsalus RP (2003) Coordinate regulation of the Escherichia coli formate
dehydrogenase fdnGHI and fdhF genes in response to nitrate, nitrite and formate: roles fro
NarL and NarP. J Bacteriol 185:5076–5085
121. Pommier J, Mandrand MA, Holt SE, Boxer DH, Giodano G (1992) A second phenazine
methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli. Biochim
Biophys Acta 1107:305–313
122. Plunkett G, Burland V, Daniels DL, Blattner FR (1993) Analysis of the Escherichia coli
genome. Nucleic Acids Res 21:3391–3398
123. Abaibou H, Pommier J, Benoit JP, Giordano G, Mandrand M (1995) Expression and
characterization of the Escherichia coli fdo locus and a possible physiological role for
aerobic formate dehydrogenase. J Bacteriol 177:7141–7149
124. Bursakov S, Liu M-Y, Payne WJ, LeGall J, Moura I, Moura JJG (1995) Isolation and
preliminary characterization of a soluble nitrate reductase from the sulfate reducing organism
Desulfovibrio desulfuricans ATCC 27774. Anaerobe 1:55–60
125. Sebban C, Blanchard L, Bruschi M, Guerlesquin F (1995) Purification and characterization
of the formate dehydrogenase from Desulfovibrio vulgaris hildenborough. FEMS Microbiol
Lett 133:143–149
126. Brondino CD, Passeggi MCG, Caldeira J, Almendra MJ, Feio MJ, Moura JJG, Moura I
(2004) Incorporation of either molybdenum or tungsten into formate dehydrogenase from
Desulfovibrio alaskensis NCIMB 13491. J Biol Inorg Chem 9:145–151
72
L. B. Maia et al.