202. Xia M, Dempski R, Hille R (1999) The reductive half-reaction of xanthine oxidase Reaction
with aldehydes and identification of the catalytically labile oxygen. J Biol Chem 274:3323–
3330
203. Boll M (2005) Key enzymes in the anaerobic aromatic metabolism catalysing birch-like
reductions. Biochim Biophys Acta 1707:34–50
204. Johannes J, Unciuleac M, Friedrich T, Warkentin E, Ermler U, Boll M (2008) Inhibitors of
the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase. Biochemistry
47:4964–4972
205. Stiefel EI (1973) Proposed molecular mechanism for the action of molybedenum in
enzymes: coupled proton and electron transfer. Proc Natl Acad Sci USA 70:988–992
206. Stiefel EI (1977) The coordination and bioinorganic chemistry of molybdenum Prog. Inorg
Chem 22:1–223
207. Rajapakshe A, Snyder RA, Astashkin AV, Bernardson P, Evans DJ, Young CG, Evans DH,
Enemark JH (2009) Insights into the nature of Mo(V) species in solution: modeling catalytic
cycles for molybdenum enzymes. Inorg Chim Acta 362:4603–4608
208. Maia L, Moura I, Moura JJG (2017) EPR spectroscopy on mononuclear
molybdenum-containing enzymes. In: Hanson G, Berliner LJ (eds) Future directions in
metalloprotein and metalloenzyme research, Biological Magnetic Resonance, vol 33.
Springer International Publishing, Cham, Chap 4, pp 55–101
209. Wilson GL, Greenwood RJ, Pilbrow JR, Spence JT, Wedd AG (1991) Molybdenum(V) sites
in xanthine oxidase and relevant analogue complexes: comparison of molybdenum-95 and
sulfur-33 coupling. J Am Chem Soc 113:6803–6812
210. Duffus BR, Schrapers P, Schuth N, Mebs S, Dau H, Leimkühler S, Haumann M (2020)
Anion binding and oxidative modification at the molybdenum cofactor of formate
dehydrogenase from Rhodobacter capsulatus studied by X-ray absorption spectroscopy.
Inorg Chem 59:214–225
211. Barber MJ, May HD, Ferry JG (1986) Inactivation of formate dehydrogenase from
methanobacterium formicicum by cyanide? Biochemistry 25(1986):8150–8155
212. Friedebold J, Bowien B (1993) Physiological and biochemical characterization of the soluble
formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus. J Bacteriol
175:4719–4728
213. George GN, Colangelo CM, Dong J, Scott RA, Khangulov SV, Gladyshev VN, Stadtman TC
(1998) X-ray absorption spectroscopy of the molybdenum site of Escherichia coli formate
dehydrogenase. J Am Chem Soc 120:1267–1273
214. George GN, Costa C, Moura JJG, Moura I (1999) Observation of ligand-based redox
chemistry at the active site of a molybdenum enzyme. J Am Chem Soc 121:2625–2626
215. Mota CS (2011) Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa,
Portugal, PhD Thesis. https://hdl.handle.net/10362/6688
216. Axley MJ, Böck A, Stadtman TC (1991) Catalytic properties of an Escherichia coli formate
dehydrogenase in which sulfur replaces selenium. Proc Natl Acad Sci USA 88:8450–8454
217. Coelho C, Gonzalez PJ, Moura JG, Moura I, Trincao J, Joao Romao M (2011) The crystal
structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states.
J Mol Biol 408:932–948
218. Cerqueira NMFSA, Fernandes PA, Gonsalez PJ, Moura JJG, Ramos MJ (2013) The sulfur
shift: an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase.
Inorg Chem 52:10766–10772
219. Robinson WE, Bassegoda A, Reisner E, Hirst J (2017) Oxidation-state-dependent binding
properties of the active site in a mo-containing formate dehydrogenase. J Am Chem Soc
139:9927–9936
220. Cornish-Bowden A (1995) Fundamentals of enzyme kinetics. Portland Press, London
221. Silveira CM, Almeida MG (2013) Small electron-transfer proteins as mediators in enzymatic
electrochemical biosensors. Anal Bioanal Chem 405:3619–3635
Carbon Dioxide Utilisation—The Formate Route
77
with aldehydes and identification of the catalytically labile oxygen. J Biol Chem 274:3323–
3330
203. Boll M (2005) Key enzymes in the anaerobic aromatic metabolism catalysing birch-like
reductions. Biochim Biophys Acta 1707:34–50
204. Johannes J, Unciuleac M, Friedrich T, Warkentin E, Ermler U, Boll M (2008) Inhibitors of
the molybdenum cofactor containing 4-hydroxybenzoyl-CoA reductase. Biochemistry
47:4964–4972
205. Stiefel EI (1973) Proposed molecular mechanism for the action of molybedenum in
enzymes: coupled proton and electron transfer. Proc Natl Acad Sci USA 70:988–992
206. Stiefel EI (1977) The coordination and bioinorganic chemistry of molybdenum Prog. Inorg
Chem 22:1–223
207. Rajapakshe A, Snyder RA, Astashkin AV, Bernardson P, Evans DJ, Young CG, Evans DH,
Enemark JH (2009) Insights into the nature of Mo(V) species in solution: modeling catalytic
cycles for molybdenum enzymes. Inorg Chim Acta 362:4603–4608
208. Maia L, Moura I, Moura JJG (2017) EPR spectroscopy on mononuclear
molybdenum-containing enzymes. In: Hanson G, Berliner LJ (eds) Future directions in
metalloprotein and metalloenzyme research, Biological Magnetic Resonance, vol 33.
Springer International Publishing, Cham, Chap 4, pp 55–101
209. Wilson GL, Greenwood RJ, Pilbrow JR, Spence JT, Wedd AG (1991) Molybdenum(V) sites
in xanthine oxidase and relevant analogue complexes: comparison of molybdenum-95 and
sulfur-33 coupling. J Am Chem Soc 113:6803–6812
210. Duffus BR, Schrapers P, Schuth N, Mebs S, Dau H, Leimkühler S, Haumann M (2020)
Anion binding and oxidative modification at the molybdenum cofactor of formate
dehydrogenase from Rhodobacter capsulatus studied by X-ray absorption spectroscopy.
Inorg Chem 59:214–225
211. Barber MJ, May HD, Ferry JG (1986) Inactivation of formate dehydrogenase from
methanobacterium formicicum by cyanide? Biochemistry 25(1986):8150–8155
212. Friedebold J, Bowien B (1993) Physiological and biochemical characterization of the soluble
formate dehydrogenase, a molybdoenzyme from Alcaligenes eutrophus. J Bacteriol
175:4719–4728
213. George GN, Colangelo CM, Dong J, Scott RA, Khangulov SV, Gladyshev VN, Stadtman TC
(1998) X-ray absorption spectroscopy of the molybdenum site of Escherichia coli formate
dehydrogenase. J Am Chem Soc 120:1267–1273
214. George GN, Costa C, Moura JJG, Moura I (1999) Observation of ligand-based redox
chemistry at the active site of a molybdenum enzyme. J Am Chem Soc 121:2625–2626
215. Mota CS (2011) Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa,
Portugal, PhD Thesis. https://hdl.handle.net/10362/6688
216. Axley MJ, Böck A, Stadtman TC (1991) Catalytic properties of an Escherichia coli formate
dehydrogenase in which sulfur replaces selenium. Proc Natl Acad Sci USA 88:8450–8454
217. Coelho C, Gonzalez PJ, Moura JG, Moura I, Trincao J, Joao Romao M (2011) The crystal
structure of Cupriavidus necator nitrate reductase in oxidized and partially reduced states.
J Mol Biol 408:932–948
218. Cerqueira NMFSA, Fernandes PA, Gonsalez PJ, Moura JJG, Ramos MJ (2013) The sulfur
shift: an activation mechanism for periplasmic nitrate reductase and formate dehydrogenase.
Inorg Chem 52:10766–10772
219. Robinson WE, Bassegoda A, Reisner E, Hirst J (2017) Oxidation-state-dependent binding
properties of the active site in a mo-containing formate dehydrogenase. J Am Chem Soc
139:9927–9936
220. Cornish-Bowden A (1995) Fundamentals of enzyme kinetics. Portland Press, London
221. Silveira CM, Almeida MG (2013) Small electron-transfer proteins as mediators in enzymatic
electrochemical biosensors. Anal Bioanal Chem 405:3619–3635
Carbon Dioxide Utilisation—The Formate Route
77