induction of the molybdenum isozyme by molybdate and constitutive synthesis of the
tungsten isozyme. Arch Microbiol 170:389–393
162. Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96:27575–27816
163. Johnson MK, Rees DC, Adams MWW (1996) Tungstoenzymes Chem Rev 96:2817–2839
164. Bevers LE, Hagedoorn PL, Hagen WR (2009) The bioinorganic chemistry of tungsten.
Coord Chem Rev 253:269–290
165. Hagen WR (2017) Tungsten-containing enzymes. 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 10, pp 313–342
166. Khangulov SVV, Gladyshev VN, Dismukes GC, Stadtman TC (1998) Selenium-containing
formate dehydrogenase H from Escherichia coli: a molybdenum enzyme that catalyzes
formate oxidation without oxygen transfer. Biochemistry 37:3518–3528
167. Thome R, Gust A, Toci R, Mendel R, Bittner F, Magalon A, Walburger A (2012) A
sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli.
J Biol Chem 287:4671–4678
168. Arnoux P, Ruppelt C, Oudouhou F, Lavergne J, Siponen MI, Toci R, Mendel RR, Bittner F,
Pignol D, Magalon A, Walburger A (2015) Sulphur shuttling across a chaperone during
molybdenum cofactor maturation. Nat Commun 6:6148
169. Schrapers P, Hartmann T, Kositzki R, Dau H, Reshke S, Schulzke C, Leimkühler S,
Haumann M (2015) Sulfido and cysteine ligation changes at the molybdenum cofactor
during substrate conversion by formate dehydrogenase (FDH) from Rhodobacter capsulatus.
Inorg Chem 54:3260–3271
170. Blanchard JS, Cleland WW (1980) Kinetic and chemical mechanisms of yeast formate
dehydrogenase. Biochemistry 19:3543–3550
171. Rotberg NS, Cleland WW (1991) Secondary 15 N isotope effects on the reactions catalyzed
by alcohol and formate dehydrogenases. Biochemistry 30:4068–4071
172. Lamzin VS, Dauter Z, Popov VO, Harutyunyan EH, Wilson KS (1994) High resolution
structures of holo and apo formate dehydrogenase. J Mol Biol 236:759–785
173. Tishkov VI, Matorin AD, Rojkova AM, Fedorchuk VV, Savitsky PA, Dementieva LA,
Lamzin VS, Mezentzev AV, Popov VO (1996) Site-directed mutagenesis of the formate
dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysis. FEBS Lett
390:104–108
174. Mesentsev AV, Lamzin VS, Tishkov VI, Ustinnikova TB, Popov VO (1997) Effect of pH on
kinetic parameters of NAD + -dependent formate dehydrogenase. Biochem J 321:475–480
175. Tishkov VI, Popov VO (2004) Catalytic mechanism and application of formate dehydrogenase. Biochemistry (Mosc) 69:1252–1267
176. Castillo R, Oliva M, Marti S, Moliner V (2008) A theoretical study of the catalytic
mechanism of formate dehydrogenase. J Phys Chem B 112:10012–10022
177. Bandaria JN, Cheatum CM, Kohen A (2009) Examination of enzymatic H-tunneling through
kinetics and dynamics. J Am Chem Soc 131:10151–10155
178. Nilov DK, Shabalin IG, Popov VO, Svedas VK (2012) Molecular modeling of formate
dehydrogenase: the formation of the Michaelis complex. J Biomol Struct Dyn 30:170–199
179. Leopoldini M, Chiodo SG, Toscano M, Russo N (2008) Reaction mechanism of
molybdoenzyme formate dehydrogenase. Chemistry 14:8674–8681
180. Mota CS, Rivas MG, Brondino CD, Moura I, Moura JJG, Gonzalez PG, Cerqueira NMFSA
(2011) The mechanism of formate oxidation by metal-dependent formate dehydrogenases.
J Biol Inorg Chem 16:1255–1268
181. Tiberti M, Papaleo E, Russo N, Gioia L, Zampella G (2012) Evidence for the formation of a
Mo-H intermediate in the catalytic cycle of formate dehydrogenase. Inorg Chem 51:8331–
8339
182. Hartmann T, Leimkuhler S (2013) The oxygen-tolerant and NAD + -dependent formate
dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO 2 to
formate. FEBS J 280:6083–6096
Carbon Dioxide Utilisation—The Formate Route
75
tungsten isozyme. Arch Microbiol 170:389–393
162. Hille R (1996) The mononuclear molybdenum enzymes. Chem Rev 96:27575–27816
163. Johnson MK, Rees DC, Adams MWW (1996) Tungstoenzymes Chem Rev 96:2817–2839
164. Bevers LE, Hagedoorn PL, Hagen WR (2009) The bioinorganic chemistry of tungsten.
Coord Chem Rev 253:269–290
165. Hagen WR (2017) Tungsten-containing enzymes. 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 10, pp 313–342
166. Khangulov SVV, Gladyshev VN, Dismukes GC, Stadtman TC (1998) Selenium-containing
formate dehydrogenase H from Escherichia coli: a molybdenum enzyme that catalyzes
formate oxidation without oxygen transfer. Biochemistry 37:3518–3528
167. Thome R, Gust A, Toci R, Mendel R, Bittner F, Magalon A, Walburger A (2012) A
sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli.
J Biol Chem 287:4671–4678
168. Arnoux P, Ruppelt C, Oudouhou F, Lavergne J, Siponen MI, Toci R, Mendel RR, Bittner F,
Pignol D, Magalon A, Walburger A (2015) Sulphur shuttling across a chaperone during
molybdenum cofactor maturation. Nat Commun 6:6148
169. Schrapers P, Hartmann T, Kositzki R, Dau H, Reshke S, Schulzke C, Leimkühler S,
Haumann M (2015) Sulfido and cysteine ligation changes at the molybdenum cofactor
during substrate conversion by formate dehydrogenase (FDH) from Rhodobacter capsulatus.
Inorg Chem 54:3260–3271
170. Blanchard JS, Cleland WW (1980) Kinetic and chemical mechanisms of yeast formate
dehydrogenase. Biochemistry 19:3543–3550
171. Rotberg NS, Cleland WW (1991) Secondary 15 N isotope effects on the reactions catalyzed
by alcohol and formate dehydrogenases. Biochemistry 30:4068–4071
172. Lamzin VS, Dauter Z, Popov VO, Harutyunyan EH, Wilson KS (1994) High resolution
structures of holo and apo formate dehydrogenase. J Mol Biol 236:759–785
173. Tishkov VI, Matorin AD, Rojkova AM, Fedorchuk VV, Savitsky PA, Dementieva LA,
Lamzin VS, Mezentzev AV, Popov VO (1996) Site-directed mutagenesis of the formate
dehydrogenase active centre: role of the His332-Gln313 pair in enzyme catalysis. FEBS Lett
390:104–108
174. Mesentsev AV, Lamzin VS, Tishkov VI, Ustinnikova TB, Popov VO (1997) Effect of pH on
kinetic parameters of NAD + -dependent formate dehydrogenase. Biochem J 321:475–480
175. Tishkov VI, Popov VO (2004) Catalytic mechanism and application of formate dehydrogenase. Biochemistry (Mosc) 69:1252–1267
176. Castillo R, Oliva M, Marti S, Moliner V (2008) A theoretical study of the catalytic
mechanism of formate dehydrogenase. J Phys Chem B 112:10012–10022
177. Bandaria JN, Cheatum CM, Kohen A (2009) Examination of enzymatic H-tunneling through
kinetics and dynamics. J Am Chem Soc 131:10151–10155
178. Nilov DK, Shabalin IG, Popov VO, Svedas VK (2012) Molecular modeling of formate
dehydrogenase: the formation of the Michaelis complex. J Biomol Struct Dyn 30:170–199
179. Leopoldini M, Chiodo SG, Toscano M, Russo N (2008) Reaction mechanism of
molybdoenzyme formate dehydrogenase. Chemistry 14:8674–8681
180. Mota CS, Rivas MG, Brondino CD, Moura I, Moura JJG, Gonzalez PG, Cerqueira NMFSA
(2011) The mechanism of formate oxidation by metal-dependent formate dehydrogenases.
J Biol Inorg Chem 16:1255–1268
181. Tiberti M, Papaleo E, Russo N, Gioia L, Zampella G (2012) Evidence for the formation of a
Mo-H intermediate in the catalytic cycle of formate dehydrogenase. Inorg Chem 51:8331–
8339
182. Hartmann T, Leimkuhler S (2013) The oxygen-tolerant and NAD + -dependent formate
dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO 2 to
formate. FEBS J 280:6083–6096
Carbon Dioxide Utilisation—The Formate Route
75