42. Yang X, Elrod LC, Reibenspies JH et al (2019) Oxygen uptake in complexes related to
[NiFeS]-and [NiFeSe]-hydrogenase active sites. Chem Sci 10:1368–1373
43. Yang X, Elrod LC, Le T et al (2019) Controlling O 2 reactivity in synthetic analogues of
[NiFeS]-and [NiFeSe]-hydrogenase active sites. J Am Chem Soc 141:15338–15347
44. Webster CE, Fan Y, Hall MB et al (2003) Experimental and computational evidence for a
boron-assisted, r-bond metathesis pathway for alkane borylation. J Am Chem Soc 125:858–
859
45. Reijerse EJ, Pham CC, Pelmenschikov V et al (2017) Direct observation of an iron-bound
terminal hydride in [FeFe]-hydrogenase by nuclear resonance vibrational spectroscopy.
J Am Chem Soc 139:4306–4309
46. Siegbahn PE, Tye JW, Hall MB (2007) Computational studies of [NiFe] and [FeFe]
hydrogenases. Chem Rev 107:4414–4435
47. Esselborn J, Muraki N, Klein K et al (2016) A structural view of synthetic cofactor
integration into [FeFe]-hydrogenases. Chem Sci 7(2):959–968
48. Siebel JF, Adamska-Venkatesh A, Weber K et al (2015) Hybrid [FeFe]-hydrogenases with
modified active sites show remarkable residual enzymatic activity. Biochemistry 54:1474–
1483
49. Berggren G, Adamska A, Lambertz C et al (2013) Biomimetic assembly and activation of
[FeFe]-hydrogenases. Nature 499:66
50. Zirngibl C, van Dongen W, Schwöre B et al (1992) H 2 -forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters
in methanogenic archaea. Eur J Biochem 208:511–520
51. Afting C, Hochheimer A, Thauer RK (1998) Function of H 2 -forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum in coenzyme F 420 reduction with H 2 . Arch Microbiol 169:206–210
52. Afting C, Kremmer E, Brucker C et al (2000) Transcriptional regulation of the synthesis of
H 2 -forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of Hmd2 and
Hmd3 in Methanothermobacter marburgensis. Arch Microbiol 174:225–232
53. Zirngibl C, Hedderich R, Thauer RK (1990) N
5
, N
10 -Methylenetetrahydromethanopterin
dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity.
FEBS Lett 261:112–116
54. Schleucher J, Griesinger C, Schwörer B, Thauer RK (1994) H 2 -forming N
5
, N
10 -
methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum catalyzes a stereoselective hydride transfer as determined by two-dimensional
NMR spectroscopy. Biochemistry 33:3986–3993
55. Klein AR, Hartmann GC, Thauer RK (1995) Hydrogen isotope effects in the reactions
catalyzed by H 2 -forming N
5
, N
10 -methylenetetrahydromethanopterin dehydrogenase from
methanogenic Archaea. Eur J Biochem 233:372–376
56. Schleucher J, Schwörer B, Thauer RK, Griesinger C (1995) Elucidation of the stereochemical course of chemical reactions by magnetic labeling. J Am Chem Soc 117:2941–2942
57. Schwörer B, Fernandez VM, Zirngibl C et al (1993) H 2 -forming N
5
, N
10 -methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum. Studies of the catalytic mechanism of the H 2 formation with hydrogen isotopes. Eur J Biochem
212:255–261
58. Hartmann GC, Santamaria E, Fernández VM, Thauer RK (1996) Studies on the catalytic
mechanism of H 2 -forming methylenetetrahydromethanopterin dehydrogenase: para-ortho H 2
conversion rates in H 2 O and D 2 O. J Biol Inorg Chem 1:446–450
59. Lyon EJ, Shima S, Boecher R et al (2004) Carbon monoxide as an intrinsic ligand to iron in
the active site of the iron-sulfur-cluster–free hydrogenase H 2 -forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. J Am Chem Soc
126:14239–14248
60. Berkessel A, Thauer RK (1995) On the mechanism of catalysis by a metal-free hydrogenase
from methanogenic Archaea: enzymatic transformation of H 2 without a metal and its
Organometallic Chemistry Control of Hydrogenases
297
[NiFeS]-and [NiFeSe]-hydrogenase active sites. Chem Sci 10:1368–1373
43. Yang X, Elrod LC, Le T et al (2019) Controlling O 2 reactivity in synthetic analogues of
[NiFeS]-and [NiFeSe]-hydrogenase active sites. J Am Chem Soc 141:15338–15347
44. Webster CE, Fan Y, Hall MB et al (2003) Experimental and computational evidence for a
boron-assisted, r-bond metathesis pathway for alkane borylation. J Am Chem Soc 125:858–
859
45. Reijerse EJ, Pham CC, Pelmenschikov V et al (2017) Direct observation of an iron-bound
terminal hydride in [FeFe]-hydrogenase by nuclear resonance vibrational spectroscopy.
J Am Chem Soc 139:4306–4309
46. Siegbahn PE, Tye JW, Hall MB (2007) Computational studies of [NiFe] and [FeFe]
hydrogenases. Chem Rev 107:4414–4435
47. Esselborn J, Muraki N, Klein K et al (2016) A structural view of synthetic cofactor
integration into [FeFe]-hydrogenases. Chem Sci 7(2):959–968
48. Siebel JF, Adamska-Venkatesh A, Weber K et al (2015) Hybrid [FeFe]-hydrogenases with
modified active sites show remarkable residual enzymatic activity. Biochemistry 54:1474–
1483
49. Berggren G, Adamska A, Lambertz C et al (2013) Biomimetic assembly and activation of
[FeFe]-hydrogenases. Nature 499:66
50. Zirngibl C, van Dongen W, Schwöre B et al (1992) H 2 -forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters
in methanogenic archaea. Eur J Biochem 208:511–520
51. Afting C, Hochheimer A, Thauer RK (1998) Function of H 2 -forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum in coenzyme F 420 reduction with H 2 . Arch Microbiol 169:206–210
52. Afting C, Kremmer E, Brucker C et al (2000) Transcriptional regulation of the synthesis of
H 2 -forming methylenetetrahydromethanopterin dehydrogenase (Hmd) and of Hmd2 and
Hmd3 in Methanothermobacter marburgensis. Arch Microbiol 174:225–232
53. Zirngibl C, Hedderich R, Thauer RK (1990) N
5
, N
10 -Methylenetetrahydromethanopterin
dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity.
FEBS Lett 261:112–116
54. Schleucher J, Griesinger C, Schwörer B, Thauer RK (1994) H 2 -forming N
5
, N
10 -
methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum catalyzes a stereoselective hydride transfer as determined by two-dimensional
NMR spectroscopy. Biochemistry 33:3986–3993
55. Klein AR, Hartmann GC, Thauer RK (1995) Hydrogen isotope effects in the reactions
catalyzed by H 2 -forming N
5
, N
10 -methylenetetrahydromethanopterin dehydrogenase from
methanogenic Archaea. Eur J Biochem 233:372–376
56. Schleucher J, Schwörer B, Thauer RK, Griesinger C (1995) Elucidation of the stereochemical course of chemical reactions by magnetic labeling. J Am Chem Soc 117:2941–2942
57. Schwörer B, Fernandez VM, Zirngibl C et al (1993) H 2 -forming N
5
, N
10 -methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum. Studies of the catalytic mechanism of the H 2 formation with hydrogen isotopes. Eur J Biochem
212:255–261
58. Hartmann GC, Santamaria E, Fernández VM, Thauer RK (1996) Studies on the catalytic
mechanism of H 2 -forming methylenetetrahydromethanopterin dehydrogenase: para-ortho H 2
conversion rates in H 2 O and D 2 O. J Biol Inorg Chem 1:446–450
59. Lyon EJ, Shima S, Boecher R et al (2004) Carbon monoxide as an intrinsic ligand to iron in
the active site of the iron-sulfur-cluster–free hydrogenase H 2 -forming methylenetetrahydromethanopterin dehydrogenase as revealed by infrared spectroscopy. J Am Chem Soc
126:14239–14248
60. Berkessel A, Thauer RK (1995) On the mechanism of catalysis by a metal-free hydrogenase
from methanogenic Archaea: enzymatic transformation of H 2 without a metal and its
Organometallic Chemistry Control of Hydrogenases
297