183. Hartmann T, Schrapers P, Utesch T, Nimtz M, Rippers Y, Dau H, Mroginski MA,
Haumann M, Leimkühler S (2016) The molybdenum active site of formate dehydrogenase is
capable of catalyzing C-H bond cleavage and oxygen atom transfer reactions. Biochemistry
55:2381–2389
184. Niks D, Duvvuru J, Escalona M, Hille R (2016) Spectroscopic and kinetic properties of the
molybdenum-containing, NAD + -dependent formate dehydrogenase from Ralstonia
eutropha. J Biol Chem 291:1162–1174
185. Dong G, Ryde U (2018) Reaction mechanism of formate dehydrogenase studied by
computational methods. J Biol Inorg Chem 23:1243–1255
186. Thauer RK, Kaufer B, Fuchs G (1975) The active species of ‘CO 2 ’ utilized by reduced
ferredoxin: CO 2 oxidoreductase from clostridium pasteurianum. Eur J Biochem 55:111–117
187. Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D (2003)
Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. Nat Struct
Biol 10:928–934
188. Tanaka R, Yamashita M, Nozaki K (2009) Catalytic hydrogenation of carbon dioxide using
Ir(III)-pincer complexes. J Am Chem Soc 131:14168–14169
189. Ziebart C, Federsel C, Anbarasan P, Jackstell R, Baumann W, Spannenberg A, Beller M
(2012) Well-defined iron catalyst for improved hydrogenation of carbon dioxide and
bicarbonate. J Am Chem Soc 134:20701–20704
190. Filonenko GA, Hensen EJM, Pidko EA (2014) Mechanism of CO 2 hydrogenation to
formates by homogeneous Ru-PNP pincer catalyst: from a theoretical description to
performance optimization. Catal Sci Technol 4:3474–3485
191. Maiti BK, Maia LB, Pal K, Pakhira B, Avilés T, Moura I, Pauleta SR, Nuñez JL, Rizzi AC,
Brondino CD, Sarkar S, Moura JJG (2014) One electron reduced square planar bis
(benzene-1,2-dithiolato) copper dianionic complex and redox switch by O 2 /HO−. Inorg
Chem 53:12799–12808
192. Lothrop AP, Snider GW, Flemer S, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ (2014)
Compensating for the absence of selenocysteine in high-molecular weight thioredoxin
reductases: the electrophilic activation hypothesis. Biochemistry 53:664–674
193. Massey V, Edmondson D (1970) On the mechanism of inactivation of xanthine oxidase by
cyanide. J Biol Chem 245:6595–6598
194. Edmondson DE, Ballou D, Vanheuvelen A, Palmer G, Massey V (1973) Kinetic studies on
the substrate reduction of xanthine oxidase. J Biol Chem 248:6135–6144
195. Olson JS, Ballou DP, Palmer G, Massey V (1974) The mechanism of action of xanthine
oxidase. J Biol Chem 249:4363–4382
196. Gutteridge S, Tanner SJ, Bray RC (1978) The molybdenum centre of native xanthine
oxidase. evidence for proton transfer from substrates to the centre and for existence of an
anion-binding site. Biochem J 175:869–878
197. Gutteridge S, Tanner SJ, Bray RC (1978) Comparison of the molybdenum centres of native
and desulpho xanthine oxidase. the nature of the cyanide-labile sulphur atom and the nature
of the proton-accepting group. Biochem J 175:887–897
198. Bray RC, Gutteridge S, Stotter DA, Tanner SJ (1979) The mechanism of xanthine oxidase
The relationship between the rapid and very rapid electron-paramagnetic-resonance signals.
Biochem J 177:357–360
199. Coughlan MP, Johnson JL, Rajagopalan KV (1980) Mechanisms of inactivation of
molybdoenzymes by cyanide. J Biol Chem 255:2694–2699
200. Gutteridg S, Bray RC (1980) Oxygen-17 splitting of the very rapid molybdenum(V) e.p.r.
signal from xanthine oxidase. rate of exchange with water of the coupled oxygen atom.
Biochem J 189:615–623
201. Malthouse JPG, Gutteridge S, Bray RC (1980) Rapid type 2 molybdenum(V)
electron-paramagnetic resonance signals from xanthine oxidase and the structure of the
active centre of the enzyme. Biochem J 185:767–770
76
L. B. Maia et al.
Haumann M, Leimkühler S (2016) The molybdenum active site of formate dehydrogenase is
capable of catalyzing C-H bond cleavage and oxygen atom transfer reactions. Biochemistry
55:2381–2389
184. Niks D, Duvvuru J, Escalona M, Hille R (2016) Spectroscopic and kinetic properties of the
molybdenum-containing, NAD + -dependent formate dehydrogenase from Ralstonia
eutropha. J Biol Chem 291:1162–1174
185. Dong G, Ryde U (2018) Reaction mechanism of formate dehydrogenase studied by
computational methods. J Biol Inorg Chem 23:1243–1255
186. Thauer RK, Kaufer B, Fuchs G (1975) The active species of ‘CO 2 ’ utilized by reduced
ferredoxin: CO 2 oxidoreductase from clostridium pasteurianum. Eur J Biochem 55:111–117
187. Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D (2003)
Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. Nat Struct
Biol 10:928–934
188. Tanaka R, Yamashita M, Nozaki K (2009) Catalytic hydrogenation of carbon dioxide using
Ir(III)-pincer complexes. J Am Chem Soc 131:14168–14169
189. Ziebart C, Federsel C, Anbarasan P, Jackstell R, Baumann W, Spannenberg A, Beller M
(2012) Well-defined iron catalyst for improved hydrogenation of carbon dioxide and
bicarbonate. J Am Chem Soc 134:20701–20704
190. Filonenko GA, Hensen EJM, Pidko EA (2014) Mechanism of CO 2 hydrogenation to
formates by homogeneous Ru-PNP pincer catalyst: from a theoretical description to
performance optimization. Catal Sci Technol 4:3474–3485
191. Maiti BK, Maia LB, Pal K, Pakhira B, Avilés T, Moura I, Pauleta SR, Nuñez JL, Rizzi AC,
Brondino CD, Sarkar S, Moura JJG (2014) One electron reduced square planar bis
(benzene-1,2-dithiolato) copper dianionic complex and redox switch by O 2 /HO−. Inorg
Chem 53:12799–12808
192. Lothrop AP, Snider GW, Flemer S, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ (2014)
Compensating for the absence of selenocysteine in high-molecular weight thioredoxin
reductases: the electrophilic activation hypothesis. Biochemistry 53:664–674
193. Massey V, Edmondson D (1970) On the mechanism of inactivation of xanthine oxidase by
cyanide. J Biol Chem 245:6595–6598
194. Edmondson DE, Ballou D, Vanheuvelen A, Palmer G, Massey V (1973) Kinetic studies on
the substrate reduction of xanthine oxidase. J Biol Chem 248:6135–6144
195. Olson JS, Ballou DP, Palmer G, Massey V (1974) The mechanism of action of xanthine
oxidase. J Biol Chem 249:4363–4382
196. Gutteridge S, Tanner SJ, Bray RC (1978) The molybdenum centre of native xanthine
oxidase. evidence for proton transfer from substrates to the centre and for existence of an
anion-binding site. Biochem J 175:869–878
197. Gutteridge S, Tanner SJ, Bray RC (1978) Comparison of the molybdenum centres of native
and desulpho xanthine oxidase. the nature of the cyanide-labile sulphur atom and the nature
of the proton-accepting group. Biochem J 175:887–897
198. Bray RC, Gutteridge S, Stotter DA, Tanner SJ (1979) The mechanism of xanthine oxidase
The relationship between the rapid and very rapid electron-paramagnetic-resonance signals.
Biochem J 177:357–360
199. Coughlan MP, Johnson JL, Rajagopalan KV (1980) Mechanisms of inactivation of
molybdoenzymes by cyanide. J Biol Chem 255:2694–2699
200. Gutteridg S, Bray RC (1980) Oxygen-17 splitting of the very rapid molybdenum(V) e.p.r.
signal from xanthine oxidase. rate of exchange with water of the coupled oxygen atom.
Biochem J 189:615–623
201. Malthouse JPG, Gutteridge S, Bray RC (1980) Rapid type 2 molybdenum(V)
electron-paramagnetic resonance signals from xanthine oxidase and the structure of the
active centre of the enzyme. Biochem J 185:767–770
76
L. B. Maia et al.