Biomimetic Hydrogenation Catalyzed by a Manganese Model of [Fe]-Hydrogenase

Article abstract of DOI:10.1002/anie.201914377

[Fe]-hydrogenase is an efficient biological hydrogenation catalyst. Despite intense research, Fe complexes mimicking the active site of [Fe]-hydrogenase have not achieved turnovers in hydrogenation reactions. Herein, we describe the design and development of a manganese(I) mimic of [Fe]-hydrogenase. This complex exhibits the highest activity and broadest scope in catalytic hydrogenation among known mimics. Thanks to its biomimetic nature, the complex exhibits unique activity in the hydrogenation of compounds analogous to methenyl-H₄MPT⁺, the natural substrate of [Fe]-hydrogenase. This activity enables asymmetric relay hydrogenation of benzoxazinones and benzoxazines, involving the hydrogenation of a chiral hydride transfer agent using our catalyst coupled to Lewis acid-catalyzed hydride transfer from this agent to the substrates.

Full text of DOI:10.1002/anie.201914377

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Accepted Article
Title: Biomimetic hydrogenation catalyzed by a manganese model of
[Fe]-hydrogenase
Authors: Huijie Pan and Xile Hu
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To be cited as: Angew. Chem. Int. Ed. 10.1002/anie.201914377
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Biomimetic hydrogenation catalyzed by a manganese model of
[Fe]-hydrogenase
Hui-Jie Pan[a] and Xile Hu*[a]
Abstract: [Fe]-hydrogenase is an efficient biological hydrogenation
catalyst. Despite intense research, Fe complexes mimicking the
active site of [Fe]-hydrogenase have not achieved turnovers in
hydrogenation reactions. Here we describe the design and
development of a manganese(I) mimic of [Fe]-hydrogenase. This
complex exhibits the highest activity and broadest scope in catalytic
hydrogenation among known mimics. Thanks to its biomimetic nature,
the complex exhibits unique activity in hydrogenation of compounds
analogous to methenyl-H4MPT+, the natural substrate of [Fe]-
hydrogenase. This activity enables asymmetric relay hydrogenation
of benzoxazinones and benzoxazines, involving hydrogenation of a
chiral hydride transfer agent using our catalyst coupled to Lewis acid-
catalyzed hydride transfer from this agent to the substrates.
anthracene-bridged NCS ligand were also active for H2
activation.[7h, 7i] Notably these two models contained a carbamoyl
donor [7c] instead of the acyl donor found in the enzyme. Among
them, the neutral derivative 3 (Fig. 1d)[7i] mediated hydrogenation
of 2,6-difluoro(phenyl)-2-(4-ethyl)imidazolium cation, a model of
methenyl-H4MPT+.[8] Despite this progress, none of the previous
Fe models achieved turnovers in hydrogenation reactions.
Catalytic hydrogenation is among the most widely used
transformations in the chemical industry. The most active and
selective hydrogenation catalysts are made of precious metals,[1]
although interest in base metal catalysts is rising.[2] Nature
provides an example of highly efficient hydrogenation catalyst
made of a base metal. [Fe]-hydrogenase[3] catalyzes the
hydrogenation of methenyl-H4MPT+ to methylene-H4MPT with a
complete stereospecificity and a high turnover frequency of up to
1900 s-1 (Fig. 1a).[4] The active site of [Fe]-hydrogenase
comprises of a low-spin Fe(II) centre coordinated by one H2O and
two cis-CO molecules, a cysteine thiolate, as well as an acyl
carbon and a pyridinyl nitrogen from a guanylylpyridinol ligand
(Fig. 1b).[4-5] The 2-OH group of the pyridonol ligand serves as an
internal base to facilitate heterolytic H2 activation upon
deprotonation.[6]
Many Fe complexes have been made to model the active site
of [Fe]-hydrogenase.[7] Among them, only few complexes could
activate H2.[6, 7g-j] Complex 1 (Fig. 1c), the best structural model, is
inactive towards H2 presumably because the 2-OH group needs
to be first deprotonated. However, 1 is unstable when treated with
a base.[7f] This complex became active only when incorporated
into the apo-enzyme of [Fe]-hydrogenase.[6] To alleviate the
stability problem associated with a 2-OH group while maintaining
a viable internal base, complex 2, which contains a robust 2-OMe
group and a basic pendant N was prepared (Fig. 1c).[7g] This
complex was indeed active for H2 activation and mediated
hydrogenation of an aldehyde. However, the Fe-acyl moiety was
prone to decomposition via decarbonylation so that catalysis
could not be achieved. Two Fe models supported by an
Figure 1. a, Enzymatic hydrogenation catalyzed by [Fe]-hydrogenase; b, Active
site of [Fe]-hydrogenase; c, Selected Fe models with a pyridinylmethylacyl
ligand; d, A selected Fe model with an anthracene-bridged carbamoyl ligand. e,
Evolution of Mn models.
Based on the isoelectronic properties of Fe(II) and Mn(I), we
recently prepared a Mn(I) model of [Fe]-hydrogenase 4 (Fig. 1e),[9]
which was active for both H2 activation and hydrogenation of
organic compounds. The Mn(I) complex was more active and
stable than its Fe(II) analogue. However, the catalytic activity and
scope remained modest. By incorporating insights learned from
the bio-mimetic chemistry of [Fe]-hydrogenase (see above), we
designed a new Mn(I) model 5 (Fig. 1e), which featured a
carbamoyl donor that was easier to access and more robust than
an acyl donor, and a basic 2-NMe2 moiety that rendered the
complex more stable than a 2-OH group. Complex 5 turned out to
be an efficient catalyst for hydrogenation of a wide range of
substrates including ketones, aldehydes, imines, as well as
enzyme substrate mimics. More importantly, complex 5 enabled
[a]
Dr. H.-J. Pan, Prof. X.L. Hu
Laboratory of Inorganic Synthesis and Catalysis, Institute of
Chemical Sciences and Engineering, École Polytechnique Fédérale
de Lausanne (EPFL), ISIC-LSCI
BCH 3305,Lausanne 1015 (Switzerland)
E-mail: xile.hu@epfl.ch
Homepage: http://lsci.epfl.ch
a
biomimetic enantioselective relay hydrogenation of
benzoxazinones and benzoxazines, yielding chiral
Supporting information for this article is given via a link at the end of
the document.
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dihydrobenzoxazinones and dihydrobenzoxazines important for
the medicinal chemistry.
needed to obtain a yield of 98% (8c). . An aliphatic ketone could
only be hydrogenated in 30% yield (8d) after 2 days. These data
suggest a modest hydridity of the Mn-H intermediate derived from
5, which react sluggishly with electron rich ketones. Consistent
with this hypothesis, hydrogenation of aldehydes was more
efficient. Both aromatic and aliphatic aldehydes were
hydrogenated in high yields (> 98%, 8e-g, 8i). A sterically
Complex 5 was prepared, in one-pot, by first deprotonation of
2-dimethylamino-6-methylaminopyridine (6) with one equivalent
o
of n-BuLi at 0 C, followed by treatment with Mn(CO)5Br (yield:
71%) (Fig. 2a). The infrared (IR) spectrum of 5 in tetrahydrofuran
(THF) exhibits three CO) peaks at 1952, 1975 and 2072 cm-1.
1
1H NMR sepctrum of 5 in THF-d8 exhibits two characteristic H
hindered
substrate,
2,4,6-trimethylbenzaldehyde,
was
peaks at 2.74 ppm and 3.15 ppm, corresponding to the 2-NMe2
proton and the 6-NMe protons, respectively. Three types of CO
carbons were observed in the 13C NMR spectrum at 216.6, 214.9,
and 213.6 ppm, and the carbamoyl carbon was observed at 218.3
ppm. These diamagnetic NMR spectra indicate a low-spin
configuration for the Mn(I) center. The solid-state molecular
structure of 5 was determined by X-ray crystallography (Fig. 2b).
The Mn ion of 5 adopts an octahedral coordination geometry, with
a bidentate NC and four CO ligands.
hydrogenated in a modest yield of 42% (8h). Hydrogenation of C-
aryl primary and secondary imines was efficient (8j-8n). For an
unknown reason, a para-Cl substitution significantly inhibited the
hydrogenation (8o). As expected, an electron-rich C-alkyl
secondary imine was a poor substrate (8p).
Figure 2. a, Synthesis of complex 5; b, X-ray structure of complex 5. The
thermal ellipsoids are displayed at 50% probability. All hydrogen atoms are
omitted for clarity. Selected bond distances (Å): Mn1-N1 2.0753(12), Mn1-C6
2.0268(14), Mn1-C10 1.7982(17), Mn1-C11 1.8674(17), Mn1-C12 1.8587(16),
Mn1-C13 1.8418(16), N2-C5 1.3696(18), N3-C1 1.4104(19), N2-C6 1.4155(18)..
Table 1. Substrate scope of hydrogenation of ketones, aldehydes, and imines
catalyzed by complex 5.
We first tested the activity of 5 in hydrogenation reactions of
common organic substrates such as aldehydes, ketones, and
imines (Table 1). Addition of N-methylpyrrolidine (MP) as base
enhanced catalytic activity. Upon optimization (for details see
table S1, SI), acetophenone was hydrogenated to 2-
phenylethanol in a yield of 91%. For comparison, hydrogenation
using complex 4 as catalyst under the same conditions only had
a 45% yield, indicating the higher catalytic activity of 5 over 4. We
further compared the catalytic efficiency of 4 and 5 for other
substrates such as 7j, and 7m (Table 1). In both cases,
significantly higher yields were obtained using 5 as catalyst. We
explored the substrate scope using 5 as catalyst. Acetophenone
analogues could be hydrogenated, but the reactions depended
strongly on the electronic properties of the substrates. Addition of
an electron donating OMe group at the para position lowered the
yield (8b) to 57%. An electron withdrawing Cl group at the para
position slowed down the hydrogenation and two days were
While the activity and scope of 5 in hydrogenation are the best
among model complexes of [Fe]-hydrogenase, they are below
those of the most active base metal catalysts for common organic
2b, 2d-f, 10]
substrates.[2a,
We considered that the strength of a
biomimetic catalyst like 5 might be its propensity to catalyze
biomimetic reactions uncommon to synthetic chemistry. In this
context, we examined the hydrogenation of substrates similar to
the native substrate of [Fe]-hydrogenase, namely, methenyl-
H4MPT+. The hydrogenation of the 1,3-bis(2,6-difluorophenyl)-2-
(4-tolyl)imidazolinium cation (in its bromide salt 9a), a previously
reported model of methenyl-H4MPT+,[7h, 8] was first tested. After
optimizing conditions (see Table S2, SI), we obtained a yield of
92% for the hydrogenation of 9a to generate 10a using 2.5 mol%
of 5 as catalyst (Scheme 1). For comparison, the previous model
4 afforded only a yield of 43% under the same conditions. We also
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tested complexes 11[11] and 12[12], which were highly active in
hydrogenation of common organic substrates. However, no
hydrogenation of 9a was observed. This result confirms our
hypothesis that biomimetic catalysts are better suited for
biomimetic reactions. We also probed the scope of hydrogenation
of other imidazolinium salts (Table 2). The Cl-substituted
analogue of 9a was hydrogenated in 80% yield (10b). The 2,6-
difluoro substituents in 9a was not essential for a substrate to be
hydrogenated. Other imidazolinium salts bearing similar N-aryl
groups such as 9c-e[13] were also good substrates of
hydrogenation, with yields of over 90%. Both electron withdrawing
Cl and electron donating OMe group were tolerated.
function of methylene-H4MPT is similar to that of NADH and
NADPH in biological hydride transfer reactions.[15] We thought
that catalyst 5 might be suitable for hydrogenation of substrates
mimicking methenyl-H4MPT+ or NAD+/NADP+, yielding hydride
donors that could further utilized for the reduction of another
unsaturated molecule. In particular,
5
might catalyze
hydrogenation of an enantiomeric pure form of a methenyl-
H4MPT+/NAD(P)/NAD(P)H mimic, leading to asymmetric
hydrogenation of a second substrate after a hydride transfer relay.
Planar-chiral FENAM 13 (a regenerable NAD(P) analogue based
on planar-chiral ferrocene) appeared to be a suitable mediator for
this relay catalysis (Scheme 2).[16] Hydrogenation of 13 catalyzed
by 5 yields 14, which can serve as a chiral hydride transfer
reagent. We chose benzoxazinones and derivatives (15) as the
terminal substrate for hydrogenation because they are
[17]
susceptible for hydride transfer reactions
and the products
dihydrobenzoxazinones are a class of important molecules in
medicinal chemistry.[18] The selectivity of a hydrogenation catalyst
towards 13 over 15 is key to the success of this relay catalysis.
Again due to the biomimetic nature of 13, we thought catalyst 5
was well suited for this applciation. Analogous relay
19]
hydrogenation was previously reported,[16,
however, Ru
complexes were mostly used for H2 activation.[16, 19a, 19b] A notable
exception was reported using an iron catalyst, but the
enantioselectivity was sub-optimal.[19c] After screening of different
conditions (Table S3, SI), we identified a protocol which reduced
benzoxazinone 15a to dihydrobenzoxazinone 16a in 63% yield
and 96% enantio excess (ee). The optimized conditions involved
10 mol% of 5 as hydrogenation catalyst, 20 mol% 13 as chiral
hydride transfer reagent, and 20 mol% La(OTf)3 as Lewis-acid.
Scheme 1. Comparison of the catalytic efficiency of various Mn complexes in
the hydrogenation of 9a, a mimic of methenyl-H4MPT+.
Scheme 2. The strategy for biomimetic asymmetric relay hydrogenation of
benzoxazinone (15) incorporating 5-catalyzed hydrogenation of enantiopure
NADP analogue 13 as a key step. The chirality of 16 was transfeered from the
chirality of 13/14.
The relay catalysis worked for the enantioselective
Table 2. Scope of hydrogenation of methenyl-H4MPT+ mimics catalyzed by
complex 5.
hydrogenation of
a wide range of substrates (Table 3).
Benzoxazinones with aromatic substitutes were all reduced with
moderate to good yields and high enantioselectivity (16a-d).
Electronic properties of the aromatic substitutes had limited effect.
Benzoxazinones with aliphatic substitutes were hydrogenated in
slightly higher yields than their aromatic counterparts (16e-h), and
again with high enantioselectivity. Comparison of ees of 16e-h
suggested that steric hindrance induced by an alkyl substituent
was beneficial for the ees. Benzoxazine substrates were
Encouraged by the above results, we considered further
applications of catalyst 5 in biomimetic hydrogenation. In nature,
hydrogenation of methenyl-H4MPT+ gave methylene-H4MPT,
which served as a hydride donor for the reduction of F420 (8-
hydroxy-5-deazaflavin) coenzyme to form F420H2, an essential
electron carrier for the hydrogenotrophic methanogenesis.[14] The
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hydrogenated cleanly and in high yields (16i-l). The
enantioselectivities of the products, however, dropped compared
to 16a-16h. These data suggest the ester group in
benzoxazinones played a role in the enantioselective hydride
transfer, probably by coordination to the Lewis acid.
Keywords: [Fe]-hydrogenase • biomimetic chemistry•
hydrogenation • manganese
[1]
a) R. Noyori, T. Ohkuma, Angew. Chem. Int. Ed. 2001, 40, 40-73; b) W.
S. Knowles, Angew. Chem. Int. Ed. 2002, 41, 1998; c) R. Noyori, Angew.
Chem. Int. Ed. 2002, 41, 2008-2022; d) J. P. Genet, Acc. Chem. Res.
2003, 36, 908.
[2]
a) T. Zell, D. Milstein, Acc. Chem. Res. 2015, 48, 1979-1994; b) R. H.
Morris, Acc. Chem. Res. 2015, 48, 1494-1502; c) M. Garbe, K. Junge, M.
Beller, Eur. J. Org. Chem. 2017, 2017, 4344-4362; d) G. A. Filonenko,
R. van Putten, E. J. M. Hensen, E. A. Pidko, Chem. Soc. Rev. 2018, 47,
1459-1483; e) F. Kallmeier, R. Kempe, Angew. Chem. Int. Ed. 2018, 57,
46-60; f) L. Alig, M. Fritz, S. Schneider, Chem. Rev. 2019, 119, 2681-
2751.
[3]
[4]
S. Shima, U. Ermler, Eur. J. Inorg. Chem. 2011, 2011, 963-972.
G. Huang, T. Wagner, M. D. Wodrich, K. Ataka, E. Bill, U. Ermler, X.
Hu, S. Shima, Nat. Catal. 2019, 2, 537-543.
[5]
a) S. Shima, O. Pilak, S. Vogt, M. Schick, M. S. Stagni, W. Meyer-
Klaucke, E. Warkentin, R. K. Thauer, U. Ermler, Science 2008, 321, 572-
575; b) T. Hiromoto, K. Ataka, O. Pilak, S. Vogt, M. S. Stagni, W.
Meyer-Klaucke, E. Warkentin, R. K. Thauer, S. Shima, U. Ermler, FEBS
Lett. 2009, 583, 585-590.
[6]
[7]
S. Shima, D. Chen, T. Xu, M. D. Wodrich, T. Fujishiro, K. M. Schultz, J.
Kahnt, K. Ataka, X. Hu, Nat. Chem. 2015, 7, 995-1002.
a) D. Schilter, J. M. Camara, M. T. Huynh, S. Hammes-Schiffer, T. B.
Rauchfuss, Chem. Rev. 2016, 116, 8693-8749; b) K. M. Schultz, D. Chen,
X. Hu, Chem. Asian J. 2013, 8, 1068-1075; c) P. J. Turrell, J. A. Wright,
J. N. T. Peck, V. S. Oganesyan, C. J. Pickett, Angew. Chem. Int. Ed.
2010, 49, 7508-7511; d) D. Chen, R. Scopelliti, X. Hu, Angew. Chem. Int.
Ed. 2011, 50, 5671-5673; e) D. Chen, R. Scopelliti, X. Hu, Angew. Chem.
Int. Ed. 2012, 51, 1919-1921; f) B. Hu, D. Chen, X. Hu, Chem. Eur. J.
2014, 20, 1677-1682; g) T. Xu, C.-J. M. Yin, M. D. Wodrich, S. Mazza,
K. M. Schultz, R. Scopelliti, X. Hu, J. Am. Chem. Soc. 2016, 138, 3270-
3273; h) J. Seo, T. A. Manes, M. J. Rose, Nat. Chem. 2017, 9, 552-557; i)
S. A. Kerns, A. C. Magtaan, P. R. Vong, M. J. Rose, Angew. Chem. Int.
Ed. 2018, 57, 2855-2858; j) Y. I. Cho, G. Durgaprasad, M. J. Rose, Inorg.
Chem. 2019, 58, 12689-12699.
Table 3. Substrate scope of biomimetic asymmetric relay hydrogenation of
benzoxazinones and benzoxazines catalyzed by complex 5. The absolute
configuration of products was assigned according to reported HPLC data.[16]
[8]
K. F. Kalz, A. Brinkmeier, S. Dechert, R. A. Mata, F. Meyer, J. Am.
Chem. Soc. 2014, 136, 16626-16634.
[9]
H.-J. Pan, G. Huang, M. D. Wodrich, F. F. Tirani, K. Ataka, S. Shima, X.
Hu, Nat. Chem. 2019, 11, 669-675.
a) D. S. Mérel, M. L. T. Do, S. Gaillard, P. Dupau, J.-L. Renaud, Coord.
Chem. Rev. 2015, 288, 50-68; b) S. Chakraborty, P. Bhattacharya, H. Dai,
H. Guan, Acc. Chem. Res. 2015, 48, 1995-2003; c) C. S. G. Seo, R. H.
Morris, Organometallics 2019, 38, 47-65.
R. van Putten, E. A. Uslamin, M. Garbe, C. Liu, A. Gonzalez-de-Castro,
M. Lutz, K. Junge, E. J. M. Hensen, M. Beller, L. Lefort, E. A. Pidko,
Angew. Chem. Int. Ed. 2017, 56, 7531-7534.
S. Elangovan, C. Topf, S. Fischer, H. Jiao, A. Spannenberg, W.
Baumann, R. Ludwig, K. Junge, M. Beller, J. Am. Chem. Soc. 2016, 138,
8809-8814.
M. Hatazawa, N. Yoshie, H. Seino, Inorg. Chem. 2017, 56, 8087-8099.
L. Bai, T. Fujishiro, G. Huang, J. Koch, A. Takabayashi, M. Yokono, A.
Tanaka, T. Xu, X. Hu, U. Ermler, S. Shima, Faraday Discuss. 2017, 198,
37-58.
a) H. Lin, Org. Biolmol. Chem. 2007, 5, 2541-2554; b) W. Ying,
Antioxid. Redox Signal. 2008, 10, 179-206; c) R. H. Houtkooper, C.
Cantꢀ, R. J. Wanders, J. Auwerx, Endocr. Rev. 2010, 31, 194-223.
J. Wang, Z.-H. Zhu, M.-W. Chen, Q.-A. Chen, Y.-G. Zhou, Angew.
Chem. Int. Ed. 2019, 58, 1813-1817.
a) M. Rueping, A. P. Antonchick, T. Theissmann, Angew. Chem. Int. Ed.
2006, 45, 6751-6755; b) R. I. Storer, D. E. Carrera, Y. Ni, D. W. C.
MacMillan, J. Am. Chem. Soc. 2006, 128, 84-86.
a) J. Ilaš, P. Š. Anderluh, M. S. Dolenc, D. Kikelj, Tetrahedron 2005, 61,
7325-7348; b) F. A. Macías, D. Marín, A. Oliveros-Bastidas, J. M. G.
Molinillo, Nat. Prod. Rep. 2009, 26, 478-489.
The mechanism of hydrogenation catalyzed by 5 is assumed
to be similar to the reaction catalyzed by the analogous catalyst
4 .[9] The detail of the mechanism, however, is subject to future
study.
[10]
[11]
[12]
In conclusion, we designed and developed a Mn(I) model of
[Fe]-hydrogenase based on insights from biomimetic chemistry of
[Fe]-hydrogenase. Key to our design was a chelating pyridine-
carbamoyl ligand with a pendant NMe2 base. This ligand was
easy to assemble and conferred improved efficiency and scope in
catalytic hydrogenation. Compared to other synthetic Mn
catalysts, our biomimetic catalyst exhibits unique activity for
hydrogenation of bio-mimetic substrates. This activity enabled an
enantioselective relay catalysis of benzoxazinones and
benzoxazines, via Mn-catalyzed hydrogtenation of an
enantiomeric pure hydride acceptor, followed by Lewis-acid
catalyzed asymmetric hydride transfer. This work demostrates the
potenital utility of biomimetic catalysts in hydrogenation reactions.
[13]
[14]
[15]
[16]
[17]
[18]
[19]
a) Q.-A. Chen, M.-W. Chen, C.-B. Yu, L. Shi, D.-S. Wang, Y. Yang, Y.-
G. Zhou, J. Am. Chem. Soc. 2011, 133, 16432-16435; b) Q.-A. Chen, K.
Gao, Y. Duan, Z.-S. Ye, L. Shi, Y. Yang, Y.-G. Zhou, J. Am. Chem. Soc.
2012, 134, 2442-2448; c) L.-Q. Lu, Y. Li, K. Junge, M. Beller, J. Am.
Chem. Soc. 2015, 137, 2763-2768; d) L. Zhao, J. Wei, J. Lu, C. He, C.
Duan, Angew. Chem. Int. Ed. 2017, 56, 8692-8696.
Acknowledgements
This work was supported by the Swiss National Science
Foundation and the European Union Marie Sklodowska-Curie
Individual Fellowships (794000). We thank Farzaneh Fadaei
Tirani and Rosario Scopelliti (EPFL) for X-ray crystallography.
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Hui-Jie Pan, and Xile Hu*
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