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34:2247–2250
61. Teles JH, Brode S, Berkessel A (1998) Hydrogenation without a metal catalyst–an ab initio
study on the mechanism of the metal-free hydrogenase from Methanobacterium thermoautotrophicum. J Am Chem Soc 120:1345–1346
62. Berkessel A (2001) Activation of dihydrogen without transition metals. Curr Opin Chem
Biol 5:486–490
63. Berkessel A, Schubert TJ, Muller TN (2002) Hydrogenation without a transition-metal
catalyst: on the mechanism of the base-catalyzed hydrogenation of ketones. J Am Chem Soc
124:8693–8698
64. Shima S, Lyon EJ, Thauer RK et al (2005) Mössbauer studies of the iron-sulfur-cluster-free
hydrogenase: the electronic state of the mononuclear fe active site. J Am Chem Soc
127:10430–10435
65. Huang G, Wagner T, Wodrich MD et al (2019) The atomic-resolution crystal structure of
activated [Fe]-hydrogenase. Nat Catal 2:537–543
66. Korbas M, Vogt S, Meyer-Klaucke W et al (2006) The iron-sulfur cluster-free hydrogenase
(Hmd) is a metalloenzyme with a novel iron binding motif. J Biol Chem 281(41):30804–
30813
67. Upadhyay V, Ceh K, Tumulka F et al (2016) Molecular characterization of Methanogenic
N
5
-Methyltetrahydromethanopterin: coenzyme M Methyltransferase. Biochim Biophys Acta
Biomembr 1858:2140–2144
68. Shima S, Pilak O, Vogt S et al (2008) The crystal structure of [Fe]-hydrogenase reveals the
geometry of the active site. Science 321:572–575
69. Hiromoto T, Ataka K, Pilak O, Vogt S et al (2009) The crystal structure of C176A mutated
[Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Lett
583:585–590
70. Hiromoto T, Warkentin E, Moll J et al (2009) The crystal structure of an [Fe]hydrogenase-substrate complex reveals the framework for H 2 activation. Angew Chem Int
Ed 48:6457–6460
71. Tamura H, Salomone-Stagni M, Fujishiro T et al (2013) Crystal structures of [Fe]hydrogenase in complex with inhibitory isocyanides: implications for the H 2 activation site.
Angew Chem Int Ed 52:9656–9659
72. Shima S, Lyon EJ, Sordel-Klippert M et al (2004) The cofactor of the iron-sulfur cluster free
hydrogenase HMD: structure of the light-inactivation product. Angew Chem Int Ed
43:2547–2551
73. Buurman G, Shima S, Thauer RK (2000) The metal-free hydrogenase from methanogenic
archaea: evidence for a bound cofactor. FEBS Lett 485:200–204
74. Ma K, Zirngibl C, Linder D et al (1991) N
5
,
N1
0-Methylenetetrahydromethanopterin
dehydrogenase ( H 2-forming) from the extreme thermophile Methanopyrus kandleri. Arch
Microbiol 156:43–48
75. Lyon EJ, Shima S, Buurman G et al (2004) UV—a/blue-light inactivation of the metal-free
hydrogenase (HMD) from methanogenic archaea: the enzyme contains functional iron after
all. Eur J Biochem 271:195–204
76. Salomone-Stagni M, Stellato F, Whaley CM et al (2010) The iron-site structure of [Fe]hydrogenase and model systems: an X-ray absorption near edge spectroscopy study. Dalton
Trans 39:3057–3064
77. Song LC, Zhu L, Hu FQ, Wang YX (2017) Studies on chemical reactivity and
electrocatalysis of two acylmethyl(hydroxymethyl)pyridine ligand-containing [Fe]-hydrogenase models (2-COCH 2 -6-HOCH 2 C 5 H 3 N)Fe(CO) 2 L (L = η
1 -SCOMe, η
1 -2- SC 5 H 4 N).
Inorg Chem 56:15216–15230
78. Pan HJ, Hu X (2020) Biomimetic hydrogenation catalyzed by a manganese model of [Fe]hydrogenase. Angew Chem 132(12):4972–4976
298
M. Y. Darensbourg et al.
34:2247–2250
61. Teles JH, Brode S, Berkessel A (1998) Hydrogenation without a metal catalyst–an ab initio
study on the mechanism of the metal-free hydrogenase from Methanobacterium thermoautotrophicum. J Am Chem Soc 120:1345–1346
62. Berkessel A (2001) Activation of dihydrogen without transition metals. Curr Opin Chem
Biol 5:486–490
63. Berkessel A, Schubert TJ, Muller TN (2002) Hydrogenation without a transition-metal
catalyst: on the mechanism of the base-catalyzed hydrogenation of ketones. J Am Chem Soc
124:8693–8698
64. Shima S, Lyon EJ, Thauer RK et al (2005) Mössbauer studies of the iron-sulfur-cluster-free
hydrogenase: the electronic state of the mononuclear fe active site. J Am Chem Soc
127:10430–10435
65. Huang G, Wagner T, Wodrich MD et al (2019) The atomic-resolution crystal structure of
activated [Fe]-hydrogenase. Nat Catal 2:537–543
66. Korbas M, Vogt S, Meyer-Klaucke W et al (2006) The iron-sulfur cluster-free hydrogenase
(Hmd) is a metalloenzyme with a novel iron binding motif. J Biol Chem 281(41):30804–
30813
67. Upadhyay V, Ceh K, Tumulka F et al (2016) Molecular characterization of Methanogenic
N
5
-Methyltetrahydromethanopterin: coenzyme M Methyltransferase. Biochim Biophys Acta
Biomembr 1858:2140–2144
68. Shima S, Pilak O, Vogt S et al (2008) The crystal structure of [Fe]-hydrogenase reveals the
geometry of the active site. Science 321:572–575
69. Hiromoto T, Ataka K, Pilak O, Vogt S et al (2009) The crystal structure of C176A mutated
[Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. FEBS Lett
583:585–590
70. Hiromoto T, Warkentin E, Moll J et al (2009) The crystal structure of an [Fe]hydrogenase-substrate complex reveals the framework for H 2 activation. Angew Chem Int
Ed 48:6457–6460
71. Tamura H, Salomone-Stagni M, Fujishiro T et al (2013) Crystal structures of [Fe]hydrogenase in complex with inhibitory isocyanides: implications for the H 2 activation site.
Angew Chem Int Ed 52:9656–9659
72. Shima S, Lyon EJ, Sordel-Klippert M et al (2004) The cofactor of the iron-sulfur cluster free
hydrogenase HMD: structure of the light-inactivation product. Angew Chem Int Ed
43:2547–2551
73. Buurman G, Shima S, Thauer RK (2000) The metal-free hydrogenase from methanogenic
archaea: evidence for a bound cofactor. FEBS Lett 485:200–204
74. Ma K, Zirngibl C, Linder D et al (1991) N
5
,
N1
0-Methylenetetrahydromethanopterin
dehydrogenase ( H 2-forming) from the extreme thermophile Methanopyrus kandleri. Arch
Microbiol 156:43–48
75. Lyon EJ, Shima S, Buurman G et al (2004) UV—a/blue-light inactivation of the metal-free
hydrogenase (HMD) from methanogenic archaea: the enzyme contains functional iron after
all. Eur J Biochem 271:195–204
76. Salomone-Stagni M, Stellato F, Whaley CM et al (2010) The iron-site structure of [Fe]hydrogenase and model systems: an X-ray absorption near edge spectroscopy study. Dalton
Trans 39:3057–3064
77. Song LC, Zhu L, Hu FQ, Wang YX (2017) Studies on chemical reactivity and
electrocatalysis of two acylmethyl(hydroxymethyl)pyridine ligand-containing [Fe]-hydrogenase models (2-COCH 2 -6-HOCH 2 C 5 H 3 N)Fe(CO) 2 L (L = η
1 -SCOMe, η
1 -2- SC 5 H 4 N).
Inorg Chem 56:15216–15230
78. Pan HJ, Hu X (2020) Biomimetic hydrogenation catalyzed by a manganese model of [Fe]hydrogenase. Angew Chem 132(12):4972–4976
298
M. Y. Darensbourg et al.