79. Kerns SK, Magtaan AC, Vong P, Rose MJ (2018) Functional Hydride transfer by a
thiolate-containing model of mono-iron hydrogenase featuring an Anthracene Scaffold.
Angew Chem Int Ed 57:2855–2858
80. Shima S, Chen D, Xu T et al (2015) Reconstitution of [Fe]-hydrogenase using model
complexes. Nat Chem 7:995–1002
81. Huang G, Wagner T, Ermler U, Shima S (2020) Methanogenesis involves direct hydride
transfer from H 2 to an organic substrate. Nat Rev Chem 4:213–221
82. Rose MJ (2020) [Fe]-Hydrogenase (HMD): insights from enzyme structure, spectroscopy
and synthetic models. In: Comprehensive coordination Chemistry III. Elsevier
83. Yang X, Hall MB (2009) Monoiron hydrogenase catalysis: hydrogen activation with the
formation of a dihydrogen, Fe–H •••H–O, bond and methenyl-H 4 MPT triggered hydride
transfer. J Am Chem Soc 131:10901–10908
84. Finkelmann AR, Senn HM, Reiher M (2014) Hydrogen-activation mechanism of [Fe]
hydrogenase revealed by multi-scale modeling. Chem Sci 5:4474–4482
85. Hedegård ED, Kongsted J, Ryde U (2015) Multiscale modeling of the active site of [Fe]
hydrogenase: the H 2 binding site in open and closed protein conformations. Angew Chem
Int Ed 54:6246–6250
86. Harris DF, Lukoyanov DA, Shaw S et al (2018) Mechanism of N 2 reduction catalyzed by
Fe-nitrogenase involves reductive elimination of H 2 . Biochemistry 57:701–771
87. Ribbe MW (Ed) (2011) Nitrogen fixation: methods and protocols. Springer
88. Sippel D, Einsle O (2017) The structure of vanadium nitrogenase reveals an unusual
bridging ligand. Nat Chem Bio 13:956
89. Hoffman BM, Lukoyanov D, Yang ZY et al (2014) Mechanism of nitrogen fixation by
nitrogenase: the next stage. Chem Rev 114:4041–4062
90. Lukoyanov D, Khadka N, Yang ZY et al (2016) Reductive elimination of H 2 activates
nitrogenase to reduce the N-N triple bond: characterization of the E4(4H) Janus intermediate
in wild-type enzyme. J Am Chem Soc 138:10674–10683
91. Hoffman BM, Lukoyanov D, Dean DR, Seefeldt LC (2013) Nitrogenase: a draft mechanism.
Acc Chem Res 46:587–595
92. Ding S, Ghosh P, Darensbourg MY, Hall MB (2017) Interplay of hemilability and redox
activity in models of hydrogenase active sites. PNAS 114:E9775–E9782
93. Matson BD, Peters JC (2018) Fe-mediated HER vs N 2 RR: exploring factors that contribute
to selectivity in P 3
E Fe(N 2 ) (E = B, Si, C) catalyst model systems. ACS Catal 8:1448–1455
94. Fan HJ, Hall MB (2001) A capable bridging ligand for Fe-only hydrogenase: density
functional calculations of a low-energy route for heterolytic cleavage and formation of
dihydrogen. J Am Chem Soc 123:3828–3829
95. Kilgore UJ, Roberts JA, Pool DH, et al (2011)[Ni(P
Ph
2 N
C6H4X
2 ) 2 ]
2+ complexes as
electrocatalysts for H 2 production: effect of substituents, acids, and water on catalytic rates.
J Am Chem Soc 133:5861–5872
96. Helm ML, Stewart MP, Bullock RM et al (2011) A synthetic nickel electrocatalyst with a
turnover frequency above 100,000 s
−1 for H 2 production. Science 333(863–866):89
97. Liu T, DuBois DL, Bullock RM (2013) An iron complex with pendent amines as a
molecular electrocatalyst for oxidation of hydrogen. Nat Chem 5:228
98. Liu T, Wang X, Hoffmann C et al (2014) Heterolytic cleavage of hydrogen by an iron
hydrogenase model: an Fe–H⋅⋅⋅ H–N dihydrogen bond characterized by neutron diffraction.
Angew Chem Int Ed 53:5300–5304
99. Dutta A, Roberts JA, Shaw WJ (2014) Arginine-containing ligands enhance H 2 oxidation
catalyst performance. Angew Chem Int Ed 53:6487–6491
100. Ginovska-Pangovska B, Dutta A, Reback ML et al (2014) Beyond the active site: the impact
of the outer coordination sphere on electrocatalysts for hydrogen production and oxidation.
Acc Chem Res 47:2621–2630
101. Darensbourg MY, Lyon EJ, Zhao X, Georgakaki IP (2003) The organometallic active site of
[Fe] hydrogenase: models and entatic states. PNAS 100:3683–3688
Organometallic Chemistry Control of Hydrogenases
299
thiolate-containing model of mono-iron hydrogenase featuring an Anthracene Scaffold.
Angew Chem Int Ed 57:2855–2858
80. Shima S, Chen D, Xu T et al (2015) Reconstitution of [Fe]-hydrogenase using model
complexes. Nat Chem 7:995–1002
81. Huang G, Wagner T, Ermler U, Shima S (2020) Methanogenesis involves direct hydride
transfer from H 2 to an organic substrate. Nat Rev Chem 4:213–221
82. Rose MJ (2020) [Fe]-Hydrogenase (HMD): insights from enzyme structure, spectroscopy
and synthetic models. In: Comprehensive coordination Chemistry III. Elsevier
83. Yang X, Hall MB (2009) Monoiron hydrogenase catalysis: hydrogen activation with the
formation of a dihydrogen, Fe–H •••H–O, bond and methenyl-H 4 MPT triggered hydride
transfer. J Am Chem Soc 131:10901–10908
84. Finkelmann AR, Senn HM, Reiher M (2014) Hydrogen-activation mechanism of [Fe]
hydrogenase revealed by multi-scale modeling. Chem Sci 5:4474–4482
85. Hedegård ED, Kongsted J, Ryde U (2015) Multiscale modeling of the active site of [Fe]
hydrogenase: the H 2 binding site in open and closed protein conformations. Angew Chem
Int Ed 54:6246–6250
86. Harris DF, Lukoyanov DA, Shaw S et al (2018) Mechanism of N 2 reduction catalyzed by
Fe-nitrogenase involves reductive elimination of H 2 . Biochemistry 57:701–771
87. Ribbe MW (Ed) (2011) Nitrogen fixation: methods and protocols. Springer
88. Sippel D, Einsle O (2017) The structure of vanadium nitrogenase reveals an unusual
bridging ligand. Nat Chem Bio 13:956
89. Hoffman BM, Lukoyanov D, Yang ZY et al (2014) Mechanism of nitrogen fixation by
nitrogenase: the next stage. Chem Rev 114:4041–4062
90. Lukoyanov D, Khadka N, Yang ZY et al (2016) Reductive elimination of H 2 activates
nitrogenase to reduce the N-N triple bond: characterization of the E4(4H) Janus intermediate
in wild-type enzyme. J Am Chem Soc 138:10674–10683
91. Hoffman BM, Lukoyanov D, Dean DR, Seefeldt LC (2013) Nitrogenase: a draft mechanism.
Acc Chem Res 46:587–595
92. Ding S, Ghosh P, Darensbourg MY, Hall MB (2017) Interplay of hemilability and redox
activity in models of hydrogenase active sites. PNAS 114:E9775–E9782
93. Matson BD, Peters JC (2018) Fe-mediated HER vs N 2 RR: exploring factors that contribute
to selectivity in P 3
E Fe(N 2 ) (E = B, Si, C) catalyst model systems. ACS Catal 8:1448–1455
94. Fan HJ, Hall MB (2001) A capable bridging ligand for Fe-only hydrogenase: density
functional calculations of a low-energy route for heterolytic cleavage and formation of
dihydrogen. J Am Chem Soc 123:3828–3829
95. Kilgore UJ, Roberts JA, Pool DH, et al (2011)[Ni(P
Ph
2 N
C6H4X
2 ) 2 ]
2+ complexes as
electrocatalysts for H 2 production: effect of substituents, acids, and water on catalytic rates.
J Am Chem Soc 133:5861–5872
96. Helm ML, Stewart MP, Bullock RM et al (2011) A synthetic nickel electrocatalyst with a
turnover frequency above 100,000 s
−1 for H 2 production. Science 333(863–866):89
97. Liu T, DuBois DL, Bullock RM (2013) An iron complex with pendent amines as a
molecular electrocatalyst for oxidation of hydrogen. Nat Chem 5:228
98. Liu T, Wang X, Hoffmann C et al (2014) Heterolytic cleavage of hydrogen by an iron
hydrogenase model: an Fe–H⋅⋅⋅ H–N dihydrogen bond characterized by neutron diffraction.
Angew Chem Int Ed 53:5300–5304
99. Dutta A, Roberts JA, Shaw WJ (2014) Arginine-containing ligands enhance H 2 oxidation
catalyst performance. Angew Chem Int Ed 53:6487–6491
100. Ginovska-Pangovska B, Dutta A, Reback ML et al (2014) Beyond the active site: the impact
of the outer coordination sphere on electrocatalysts for hydrogen production and oxidation.
Acc Chem Res 47:2621–2630
101. Darensbourg MY, Lyon EJ, Zhao X, Georgakaki IP (2003) The organometallic active site of
[Fe] hydrogenase: models and entatic states. PNAS 100:3683–3688
Organometallic Chemistry Control of Hydrogenases
299