49. Canaguier S, Field M, Oudart Y, Pecaut J, Fontecave M, Artero V (2010) A structural and
functional mimic of the active site of NiFe hydrogenases. Chem Commun 46(32):5876–5878.
doi:10.1039/c001675f
50. Cui H-H, Wang J-Y, Hu M-Q, Ma C-B, Wen H-M, Song X-W, Chen C-N (2013) Efficient
photo-driven hydrogen evolution by binuclear nickel catalysts of different coordination in
noble-metal-free systems. Dalton Trans 42(24):8684–8691. doi:10.1039/c3dt50140j
51. Barton BE, Rauchfuss TB (2010) Hydride-containing models for the active site of the nickeliron hydrogenases. J Am Chem Soc 132(42):14877–14885. doi:10.1021/ja105312p
52. Carroll ME, Barton BE, Gray DL, Mack AE, Rauchfuss TB (2011) Active-site models for the
nickel–iron hydrogenases: effects of ligands on reactivity and catalytic properties. Inorg
Chem 50(19):9554–9563. doi:10.1021/ic2012759
53. Huynh MT, Schilter D, Hammes-Schiffer S, Rauchfuss TB (2014) Protonation of nickel–iron
hydrogenase models proceeds after isomerization at nickel. J Am Chem Soc 136
(35):12385–12395. doi:10.1021/ja505783z
54. Tard C, Pickett CJ (2009) Structural and functional analogues of the active sites of the [Fe]-,
[NiFe]-, and [FeFe]-hydrogenases. Chem Rev 109(6):2245–2274. doi:10.1021/cr800542q
55. Darensbourg MY, Lyon EJ, Zhao X, Georgakaki IP (2003) The organometallic active site of
[Fe]-hydrogenase: models and entatic states. Proc Natl Acad Sci U S A 100(7):3683–3688.
doi:10.1073/pnas.0536955100
56. Roy S, Groy TL, Jones AK (2013) Biomimetic model for [FeFe]-hydrogenase: asymmetrically disubstituted diiron complex with a redox-active 2,2
0 -bipyridyl ligand. Dalton Trans 42
(11):3843–3853. doi:10.1039/c2dt32457a
57. Roy S, Mazinani SKS, Groy TL, Gan L, Tarakeshwar P, Mujica V, Jones AK (2014)
Catalytic hydrogen evolution by Fe(II) carbonyls featuring a dithiolate and a chelating
phosphine. Inorg Chem 53(17):8919–8929. doi:10.1021/ic5012988
58. Lansing JC, Camara JM, Gray DE, Rauchfuss TB (2014) Hydrogen production catalyzed by
bidirectional, biomimetic models of the [FeFe]-hydrogenase active site. Organometallics 33
(20):5897–5906. doi:10.1021/om5004013
59. Liu T, Darensbourg MY (2007) A mixed-valent, Fe(II)Fe(I), diiron complex reproduces the
unique rotated state of the [FeFe]-hydrogenase active site. J Am Chem Soc 129
(22):7008–7009. doi:10.1021/ja071851a
60. Justice AK, Rauchfuss TB, Wilson SR (2007) Unsaturated, mixed-valence diiron dithiolate
model for the H-ox state of the [FeFe]-hydrogenase. Angew Chem Int Ed 46(32):6152–6154.
doi:10.1002/anie.200702224
61. Singleton ML, Bhuvanesh N, Reibenspies JH, Darensbourg MY (2008) Synthetic support of
de novo design: sterically bulky [FeFe]-hydrogenase models. Angew Chem Int Ed 47
(49):9492–9495. doi:10.1002/anie.200803939
62. Munery S, Capon J-F, De Gioia L, Elleouet C, Greco C, Pe ´tillon FY, Schollhammer P,
Talarmin J, Zampella G (2013) New Fe(I)-Fe(I) complex featuring a rotated conformation
related to the [2Fe](H) subsite of [FeFe]-hydrogenase. Chemistry 19(46):15458–15461.
doi:10.1002/chem.201303316
63. Olsen MT, Bruschi M, De Gioia L, Rauchfuss TB, Wilson SR (2008) Nitrosyl derivatives of
diiron(I) dithiolates mimic the structure and Lewis acidity of the [FeFe]-hydrogenase active
site. J Am Chem Soc 130(36):12021–12030. doi:10.1021/ja802268p
64. Hsieh C-H, Erdem OF, Harman SD, Singleton ML, Reijerse E, Lubitz W, Popescu CV,
Reibenspies JH, Brothers SM, Hall MB, Darensbourg MY (2012) Structural and spectroscopic features of mixed valent Fe(II)Fe(I) complexes and factors related to the rotated
configuration of diiron hydrogenase. J Am Chem Soc 134(31):13089–13102. doi:10.1021/
ja304866r
65. Singleton ML, Reibenspies JH, Darensbourg MY (2010) A cyclodextrin host/guest approach
to a hydrogenase active site biomimetic cavity. J Am Chem Soc 132(26):8870–8871.
doi:10.1021/ja103774j
Biomimetic Complexes for Production of Dihydrogen and Reduction of CO 2
265
functional mimic of the active site of NiFe hydrogenases. Chem Commun 46(32):5876–5878.
doi:10.1039/c001675f
50. Cui H-H, Wang J-Y, Hu M-Q, Ma C-B, Wen H-M, Song X-W, Chen C-N (2013) Efficient
photo-driven hydrogen evolution by binuclear nickel catalysts of different coordination in
noble-metal-free systems. Dalton Trans 42(24):8684–8691. doi:10.1039/c3dt50140j
51. Barton BE, Rauchfuss TB (2010) Hydride-containing models for the active site of the nickeliron hydrogenases. J Am Chem Soc 132(42):14877–14885. doi:10.1021/ja105312p
52. Carroll ME, Barton BE, Gray DL, Mack AE, Rauchfuss TB (2011) Active-site models for the
nickel–iron hydrogenases: effects of ligands on reactivity and catalytic properties. Inorg
Chem 50(19):9554–9563. doi:10.1021/ic2012759
53. Huynh MT, Schilter D, Hammes-Schiffer S, Rauchfuss TB (2014) Protonation of nickel–iron
hydrogenase models proceeds after isomerization at nickel. J Am Chem Soc 136
(35):12385–12395. doi:10.1021/ja505783z
54. Tard C, Pickett CJ (2009) Structural and functional analogues of the active sites of the [Fe]-,
[NiFe]-, and [FeFe]-hydrogenases. Chem Rev 109(6):2245–2274. doi:10.1021/cr800542q
55. Darensbourg MY, Lyon EJ, Zhao X, Georgakaki IP (2003) The organometallic active site of
[Fe]-hydrogenase: models and entatic states. Proc Natl Acad Sci U S A 100(7):3683–3688.
doi:10.1073/pnas.0536955100
56. Roy S, Groy TL, Jones AK (2013) Biomimetic model for [FeFe]-hydrogenase: asymmetrically disubstituted diiron complex with a redox-active 2,2
0 -bipyridyl ligand. Dalton Trans 42
(11):3843–3853. doi:10.1039/c2dt32457a
57. Roy S, Mazinani SKS, Groy TL, Gan L, Tarakeshwar P, Mujica V, Jones AK (2014)
Catalytic hydrogen evolution by Fe(II) carbonyls featuring a dithiolate and a chelating
phosphine. Inorg Chem 53(17):8919–8929. doi:10.1021/ic5012988
58. Lansing JC, Camara JM, Gray DE, Rauchfuss TB (2014) Hydrogen production catalyzed by
bidirectional, biomimetic models of the [FeFe]-hydrogenase active site. Organometallics 33
(20):5897–5906. doi:10.1021/om5004013
59. Liu T, Darensbourg MY (2007) A mixed-valent, Fe(II)Fe(I), diiron complex reproduces the
unique rotated state of the [FeFe]-hydrogenase active site. J Am Chem Soc 129
(22):7008–7009. doi:10.1021/ja071851a
60. Justice AK, Rauchfuss TB, Wilson SR (2007) Unsaturated, mixed-valence diiron dithiolate
model for the H-ox state of the [FeFe]-hydrogenase. Angew Chem Int Ed 46(32):6152–6154.
doi:10.1002/anie.200702224
61. Singleton ML, Bhuvanesh N, Reibenspies JH, Darensbourg MY (2008) Synthetic support of
de novo design: sterically bulky [FeFe]-hydrogenase models. Angew Chem Int Ed 47
(49):9492–9495. doi:10.1002/anie.200803939
62. Munery S, Capon J-F, De Gioia L, Elleouet C, Greco C, Pe ´tillon FY, Schollhammer P,
Talarmin J, Zampella G (2013) New Fe(I)-Fe(I) complex featuring a rotated conformation
related to the [2Fe](H) subsite of [FeFe]-hydrogenase. Chemistry 19(46):15458–15461.
doi:10.1002/chem.201303316
63. Olsen MT, Bruschi M, De Gioia L, Rauchfuss TB, Wilson SR (2008) Nitrosyl derivatives of
diiron(I) dithiolates mimic the structure and Lewis acidity of the [FeFe]-hydrogenase active
site. J Am Chem Soc 130(36):12021–12030. doi:10.1021/ja802268p
64. Hsieh C-H, Erdem OF, Harman SD, Singleton ML, Reijerse E, Lubitz W, Popescu CV,
Reibenspies JH, Brothers SM, Hall MB, Darensbourg MY (2012) Structural and spectroscopic features of mixed valent Fe(II)Fe(I) complexes and factors related to the rotated
configuration of diiron hydrogenase. J Am Chem Soc 134(31):13089–13102. doi:10.1021/
ja304866r
65. Singleton ML, Reibenspies JH, Darensbourg MY (2010) A cyclodextrin host/guest approach
to a hydrogenase active site biomimetic cavity. J Am Chem Soc 132(26):8870–8871.
doi:10.1021/ja103774j
Biomimetic Complexes for Production of Dihydrogen and Reduction of CO 2
265