A [NiFe]hydrogenase model that catalyses the release of hydrogen from formic acid

Article abstract of DOI:10.1039/c4cc05911e

We report the decomposition of formic acid to hydrogen and carbon dioxide, catalysed by a NiRu complex originally developed as a [NiFe]hydrogenase model. This is the first example of H₂ evolution, catalysed by a [NiFe]hydrogenase model, which does not require additional energy.

Full text of DOI:10.1039/c4cc05911e

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A [NiFe]hydrogenase model that catalyses the
release of hydrogen from formic acid†
Cite this: Chem. Commun., 2014,
0, 13385
5
abc
bc
abc
abc
Nga T. Nguyen,
Yuki Mori, Takahiro Matsumoto,
Takeshi Yatabe,
b
ab
ac
abc
Received 30th July 2014,
Accepted 9th September 2014
Ryota Kabe, Hidetaka Nakai, Ki-Seok Yoon and Seiji Ogo*
DOI: 10.1039/c4cc05911e
www.rsc.org/chemcomm
We report the decomposition of formic acid to hydrogen and
carbon dioxide, catalysed by a NiRu complex originally developed
as a [NiFe]hydrogenase model. This is the first example of H
2
evolution, catalysed by a [NiFe]hydrogenase model, which does
not require additional energy.
1
An enzyme complex, formate hydrogen lyase (FHL, Fig. 1),
2
catalyses H evolution from HCOOH (eqn (1)). This complex is
2
constructed from a formate dehydrogenase (FDH), which
catalyses the extraction of protons and electrons from HCOOH
3
(
eqn (2)), and a [NiFe]hydrogenase ([NiFe]H ase), which
2
recombines those protons and electrons into H
2
(eqn (3)). It
should be noted that this latter process is the reverse of the
3
usual role of [NiFe]H
2
ase in natural organisms.
Fig. 1 A structure of formate hydrogen lyase (FHL) constructed from a
FHL
2
[NiFe]hydrogenase ([NiFe]H ase) and a formate dehydrogenase (FDH). The
ꢀ
!
HCOOH
ꢀ
CO2 þH2
(1)
(2)
(3)
HycB, C, D, F and G polypeptides are membrane-integral electron transfer
components. The gray-shaded component is the membrane. (Adapted
from ref. 1a).
FDH
HCOOH
ꢀ
CO2 þ2H þ2eꢀ
þ
ꢀ!
½NiFeꢁH2ase
ꢀ
þ
ꢀ
!
ꢀ
2
H þ2e
H2
Here, we report the first catalyst that is capable of both
heterolytically splitting dihydrogen into protons and electrons
Two [NiFe]H
2
ase model complexes have been reported so
far, a NiFe catalyst by Rauchfuss et al. that requires additional
and decomposing formic acid into CO
2 2
and H . Furthermore,
this catalyst needs no additional energy to achieve useful rates.
4
electrical energy and a NiFe
2
catalyst by Schr o¨ der et al. that
II
II
II
II
6
A m-hydrido Ni Ru complex, [Ni L(H O)(m-H)Ru (Z -C Me )]-
2
6
6
5
requires additional light energy. Since we have developed a
successful [NiFe]H ase model catalyst, we felt that it would be
a good candidate for a FHL model system, which proved to be
0
NO ) {[2](NO ), L = N,N -dimethyl-3,7-diazanonane-1,9-dithiolato},
3 3
(
6
2
reacts with one equivalent of HCOONa in water to produce a
II
II
II
II
(
(
(
m-hydrido)(formato) Ni Ru complex, [Ni L(HCOO)(m-H)Ru -
7
the case.
6
Z -C
6
Me
6
)] (1), which was followed by UV-vis spectroscopy
ꢀ
Fig. S1, ESI†). The H
2
O ligand was replaced with HCOO , which
a
Centre for Small Molecule Energy, Kyushu University, 744 Moto-oka,
is coordinated to the Ni centre as an axial ligand. The structure
of 1 has been unequivocally determined by X-ray analysis (Fig. 2)
as well as positive- and negative-ion electrospray ionization mass
spectrometry (ESI-MS) (Fig. S2 and S3, ESI†) and IR spectroscopy
Nishi-ku, Fukuoka 819-0395, Japan. E-mail: ogo.seiji.872@m.kyushu-u.ac.jp;
Fax: +81-92-802-2823; Tel: +81-92-802-2818
b
Department of Chemistry and Biochemistry, Graduate School of Engineering,
Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan
c
International Institute for Carbon-Neutral Energy Research (WPI-I2CNER),
(Fig. S4, ESI†).
Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan
A brown crystal of 1 was obtained from its aqueous solution.
†
Electronic supplementary information (ESI) available: Experimental details and
2
The framework of 1 is based around a NiS Ru butterfly core
with a bridging hydride (Fig. 2). The Ni atom adopts distorted
Fig. S1–S4. CCDC 1016741. For ESI and crystallographic data in CIF or other
electronic format see DOI: 10.1039/c4cc05911e
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Fig. 3 pH-dependent
H
2
evolution catalysed by
2
(7.3 nmol) with
Fig. 2 An ORTEP drawing of 1 with ellipsoids at 50% probability. The
HCOONa (146 mmol) in water (510 mL) for 1 h at 60 1C. The maximum
turnover number (TON) is 857 at pH 3.5.
0
solvents (H
diazanonane-1,9-dithiolato) and C
interatomic distances (l/Å) and angles (f/1): Ni1–H1 = 1.88(6), Ru1–H1 =
.61(6), Ni1ꢂꢂꢂRu1 = 2.7780(11), Ni1–S1 = 2.3676(19), Ni1–S2 = 2.3818(19),
Ni1–O1 = 2.060(5), Ni1–N1 = 2.125(6), Ni1–N2 = 2.120(6), Ru1–S1 =
.4084(17), Ru1–S2 = 2.3939(17), Ni1–S1–Ru1 = 71.13(5), and Ni1–S2–Ru1 =
1.14(5).
2
O) and hydrogen atoms of ligands L (N,N -dimethyl-3,7-
6
Me are omitted for clarity. Selected
6
1
2
7
octahedral coordination that consists of the hydrido and
formato ligands at the axial site and the N donor ligand at
the equatorial site. The Ni–S–Ru angles are 71.13(5)1 and
1.14(5)1, which are comparable to those of the m-hydrido
2 2
S
7
II
II
6
Ni Ru complex 2 {70.7(3)1 and 70.4(2)1}. The NiꢂꢂꢂRu distance
of 2.7780(11) Å is also comparable to that of 2 {2.739(3) Å}.
A positive-ion ESI mass spectrum of 1 exhibits a prominent
signal at m/z 543.2 {relative intensity (I) = 100% in the range m/z
200–2000} (Fig. S2, ESI†). The signal has a characteristic
isotopic distribution that matches well with the calculated
+
isotopic distribution for [1 ꢀHCOO] , which shifts to m/z
2
Fig. 4 A proposed mechanism for H evolution from HCOOH catalysed
II
II
6
5
6 6
44.2 by the use of [Ni L(DCOO)(m-D)Ru (Z -C Me )] (double
by NiRu complexes in acidic media.
D-labelled 1). A negative-ion ESI mass spectrum of 1 shows a
ꢀ
HCOO adduct, which displays a prominent signal at m/z 633.2
(
I = 100% in the range m/z 200–2000) (Fig. S3, ESI†), whose
2
A proposed mechanism for H evolution from HCOOH
II
II
characteristic isotopic distribution matches well with the catalysed by 1 is shown in Fig. 4. The m-hydrido Ni Ru
calculated isotopic distribution for [1 + HCOO] . The signal complex 2 reacts with HCOO to form the (m-hydrido)-
shifts to m/z 636.3 by using double D-labelled 1. An IR spectrum (formato) Ni Ru complex 1. Liberation of CO
of 1 shows isotope-sensitive bands at 1349, 1760 and 2649 cm
ꢀ
ꢀ
II
II
2
from 1 affords
a dihydrido intermediate A and then reductive elimination of
2
H from A yields the low-valent species B. The species B
ꢀ
1
,
ꢀ1
which shift to 1329, 1248 and 2114 cm , respectively, after
isotopic substitution of H by D in the hydrido and formato reduces H to reform 2. This reaction mechanism is the same
positions (Fig. S4, ESI†). as the H activation mechanism by 2 except that HCOOH is
The (m-hydrido)(formato) Ni Ru complex 1 catalysed H
CO evolution from HCOOH in acidic media (pH 2.5–6.0). H
CO gases were detected by GC. Fig. 3 shows a pH-dependent catalysed by a NiRu complex without any need for additional
profile of turnover numbers (TONs, mol of H evolved/mol of energy input. Furthermore, we have structurally defined the
catalyst) of the H evolution from HCOOH for 1 h at 60 1C. The reaction intermediate of the (m-hydrido)(formato) Ni Ru
rate of H evolution examined in this study shows a maximum complex during catalytic H evolution.
around pH 3.5. The pH dependence should be explained by a This work was supported by Grants-in-Aid 26000008 (Specially
+
2
II
II
8
2
and used instead of H
2
.
2
2
and In conclusion, we have achieved H evolution from HCOOH
2
2
2
II
II
2
2
2
protonation process of a proposed low-valent species B (see Fig. 4) promoted Research), 26810038, 26410074, 25620047, 25248017,
and by the stability of the complex, i.e., the species is decomposed and 24109016 from the Ministry of Education, Culture, Sports,
to unidentified mononuclear species below pH 3.0. It was Science and Technology (MEXT), Japan, the World Premier
confirmed that the reaction of 2 with H
range of pH 2.0–9.0 at room temperature did not afford 1.
2
and CO
2
in H
2
O in the International Research Centre Initiative (WPI), and the Basic
Research Programs CREST Type from JST, Japan.
1
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