hydrogenase HydA1 from Chlamydomonas reinhardtii. J Am Chem Soc 135:6921–6929.
doi:10.1021/ja4000257
18. Evans RM, Parkin A, Roessler MM, Murphy BJ, Adamson H, Lukey MJ, Sargent F,
Volbeda A, Fontecilla-Camps JC, Armstrong FA (2013) Principles of sustained enzymatic
hydrogen oxidation in the presence of oxygen - the crucial influence of high potential Fe-S
clusters in the electron relay of [NiFe]-hydrogenases. J Am Chem Soc 135:2694–2707.
doi:10.1021/ja311055d
19. Lemon BJ, Peters JW (1999) Binding of exogenously added carbon monoxide at the active
site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum. Biochemistry 38
(40):12969–12973. doi:10.1021/bi9913193
20. Pandelia ME, Ogata H, Lubitz W (2010) Intermediates in the catalytic cycle of [NiFe]
hydrogenase: functional spectroscopy of the active site. ChemPhysChem 11:1127–1140.
doi:10.1002/cphc.200900950
21. Shafaat HS, Rudiger O, Ogata H, Lubitz W (2013) [NiFe]-hydrogenases: a common active
site for hydrogen metabolism under diverse conditions. Bioenergetics 1827:986–1002.
doi:10.1016/j.bbabio.2013.01.015
22. Ogata H, Hirota S, Nakahara A, Komori H, Shibata N, Kato T, Kano K, Higuchi Y (2005)
Activation process of [NiFe]-hydrogenase elucidated by high-resolution X-Ray analyses:
conversion of the ready to the unready state. Structure 13:1635–1642. doi:10.1016/j.str.2005.
07.018
23. Montet Y, Amara P, Volbeda A, Vernede X, Hatchikian EC, Field MJ, Frey M, FontecillaCamps JC (1997) Gas access to the active site of [NiFe]-hydrogenases probed by X-Ray
crystallography and molecular dynamics. Nat Struct Mol Biol 4:523–526. doi:10.1038/
nsb0797-523
24. Liebgott PP, de Lacey AL, Burlat B, Cournac L, Richaud P, Brugna M, Fernandez VM,
Guigliarelli B, Rousset M, Le ´ger C, Dementin S (2011) Original design of an oxygen-tolerant
[NiFe]-hydrogenase: major effect of a valine-to-cysteine mutation near the active site. J Am
Chem Soc 133:986–997. doi:10.1021/ja108787s
25. Volbeda A, Amara P, Darnault C, Mouesca J-M, Parkin A, Roessler MM, Armstrong FA,
Fontecilla-Camps JC (2012) X-Ray crystallographic and computational studies of the
O 2 -tolerant [NiFe]-hydrogenase 1 from Escherichia coli. Proc Natl Acad Sci U S A
109:5305–5310. doi:10.1073/pnas.1119806109
26. Pandelia M-E, Bykov D, Izsak R, Infossi P, Giudici-Orticoni M-T, Bill E, Neese F, Lubitz W
(2013) Electronic structure of the unique [4Fe-3S] cluster in O 2 -tolerant hydrogenases
characterized by
57
Fe m€ ossbauer and EPR spectroscopy. Proc Natl Acad Sci U S A
110:483–488. doi:10.1073/pnas.1202575110
27. Dementin S, Burlat B, De Lacey AL, Pardo A, Adryanczyk-Perrier G, Guigliarelli B,
Fernandez VM, Rousset M (2004) A glutamate is the essential proton transfer gate during
the catalytic cycle of the [NiFe]-hydrogenase. J Biol Chem 279:10508–10513. doi:10.1074/
jbc.M312716200
28. Appel AM, Bercaw JE, Bocarsly AB, Dobbek H, DuBois DL, Dupuis M, Ferry JG, Fujita E,
Hille R, Kenis PJA, Kerfeld CA, Morris RH, Peden CHF, Portis AR, Ragsdale SW,
Rauchfuss TB, Reek JNH, Seefeldt LC, Thauer RK, Waldrop GL (2013) Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO 2 fixation. Chem Rev
113:6621–6658. doi:10.1021/cr300463y
29. Can M, Armstrong FA, Ragsdale SW (2014) Structure, function, and mechanism of the nickel
metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase. Chem Rev 114:4149–4174.
doi:10.1021/cr400461p
30. Svetlitchnyi V, Peschel C, Acker G, Meyer O (2001) Two membrane-associated [NiFeS]carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans. J Bacteriol 183:5134–5144. doi:10.1128/jb.183.
17.5134-5144.2001
Biomimetic Complexes for Production of Dihydrogen and Reduction of CO 2
263
doi:10.1021/ja4000257
18. Evans RM, Parkin A, Roessler MM, Murphy BJ, Adamson H, Lukey MJ, Sargent F,
Volbeda A, Fontecilla-Camps JC, Armstrong FA (2013) Principles of sustained enzymatic
hydrogen oxidation in the presence of oxygen - the crucial influence of high potential Fe-S
clusters in the electron relay of [NiFe]-hydrogenases. J Am Chem Soc 135:2694–2707.
doi:10.1021/ja311055d
19. Lemon BJ, Peters JW (1999) Binding of exogenously added carbon monoxide at the active
site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum. Biochemistry 38
(40):12969–12973. doi:10.1021/bi9913193
20. Pandelia ME, Ogata H, Lubitz W (2010) Intermediates in the catalytic cycle of [NiFe]
hydrogenase: functional spectroscopy of the active site. ChemPhysChem 11:1127–1140.
doi:10.1002/cphc.200900950
21. Shafaat HS, Rudiger O, Ogata H, Lubitz W (2013) [NiFe]-hydrogenases: a common active
site for hydrogen metabolism under diverse conditions. Bioenergetics 1827:986–1002.
doi:10.1016/j.bbabio.2013.01.015
22. Ogata H, Hirota S, Nakahara A, Komori H, Shibata N, Kato T, Kano K, Higuchi Y (2005)
Activation process of [NiFe]-hydrogenase elucidated by high-resolution X-Ray analyses:
conversion of the ready to the unready state. Structure 13:1635–1642. doi:10.1016/j.str.2005.
07.018
23. Montet Y, Amara P, Volbeda A, Vernede X, Hatchikian EC, Field MJ, Frey M, FontecillaCamps JC (1997) Gas access to the active site of [NiFe]-hydrogenases probed by X-Ray
crystallography and molecular dynamics. Nat Struct Mol Biol 4:523–526. doi:10.1038/
nsb0797-523
24. Liebgott PP, de Lacey AL, Burlat B, Cournac L, Richaud P, Brugna M, Fernandez VM,
Guigliarelli B, Rousset M, Le ´ger C, Dementin S (2011) Original design of an oxygen-tolerant
[NiFe]-hydrogenase: major effect of a valine-to-cysteine mutation near the active site. J Am
Chem Soc 133:986–997. doi:10.1021/ja108787s
25. Volbeda A, Amara P, Darnault C, Mouesca J-M, Parkin A, Roessler MM, Armstrong FA,
Fontecilla-Camps JC (2012) X-Ray crystallographic and computational studies of the
O 2 -tolerant [NiFe]-hydrogenase 1 from Escherichia coli. Proc Natl Acad Sci U S A
109:5305–5310. doi:10.1073/pnas.1119806109
26. Pandelia M-E, Bykov D, Izsak R, Infossi P, Giudici-Orticoni M-T, Bill E, Neese F, Lubitz W
(2013) Electronic structure of the unique [4Fe-3S] cluster in O 2 -tolerant hydrogenases
characterized by
57
Fe m€ ossbauer and EPR spectroscopy. Proc Natl Acad Sci U S A
110:483–488. doi:10.1073/pnas.1202575110
27. Dementin S, Burlat B, De Lacey AL, Pardo A, Adryanczyk-Perrier G, Guigliarelli B,
Fernandez VM, Rousset M (2004) A glutamate is the essential proton transfer gate during
the catalytic cycle of the [NiFe]-hydrogenase. J Biol Chem 279:10508–10513. doi:10.1074/
jbc.M312716200
28. Appel AM, Bercaw JE, Bocarsly AB, Dobbek H, DuBois DL, Dupuis M, Ferry JG, Fujita E,
Hille R, Kenis PJA, Kerfeld CA, Morris RH, Peden CHF, Portis AR, Ragsdale SW,
Rauchfuss TB, Reek JNH, Seefeldt LC, Thauer RK, Waldrop GL (2013) Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO 2 fixation. Chem Rev
113:6621–6658. doi:10.1021/cr300463y
29. Can M, Armstrong FA, Ragsdale SW (2014) Structure, function, and mechanism of the nickel
metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase. Chem Rev 114:4149–4174.
doi:10.1021/cr400461p
30. Svetlitchnyi V, Peschel C, Acker G, Meyer O (2001) Two membrane-associated [NiFeS]carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans. J Bacteriol 183:5134–5144. doi:10.1128/jb.183.
17.5134-5144.2001
Biomimetic Complexes for Production of Dihydrogen and Reduction of CO 2
263