ORI GI NAL PAPER

Designing Heterogeneous Catalysts by Incorporating

Enzyme-Like Functionalities into MOFs
Karl Petter Lillerud

Unni Olsbye

Mats Tilset
Published online: 8 May 2010
Springer Science+Business Media, LLC 2010
Abstract Everyone who works within the eld of catal-
ysis draws inspiration from the amazing functionality of
natures catalysts, the enzymes. It is particularly the mild
conditions that these catalysts are able to operate at and the
selectivity that they demonstrate that make these materials
dream targets for scientists involved in the art of synthe-
sizing homogeneous and heterogeneous industrial cata-
lysts. But enzymes also have their weak points; in
particular their low thermal stability and their often too
slow reaction rates for an economical industrial process are
problems that have to be overcome. The obvious solution
would be to copy the catalytic active center into a robust
open framework. A key property of an enzyme is its
selectivity; this property is partly regulated by steric con-
straints surrounding the catalytically active site. The
microporous zeolite based catalysts in some cases show
impressive selectivity based on the geometrical constraints
imposed by the size and shape of the regular channels in
these crystalline silicate and alumino-phosphate based
structures, and enzyme-like properties have been claimed
but the pure inorganic nature of the selective internal sur-
face in these materials makes it impossible to mimic many
important enzymatic properties. The new generation of
microporous materials, Metal Organic Frameworks
(MOFs) are hybrids of organic and inorganic structures.
This dualistic nature offers an unprecedented exibility in
the possibility to incorporate both organic and metallic
functional groups into the ordered crystalline lattice and
thereby opening up for a much greater possibility to copy
structural motifs known from enzymes into much simpler
but also more stable open structures. Several groups are
working on development of new catalysts by this approach.
Here we will illustrate this approach with structures that
mimic anhydrase and CH activation.
Keywords Metal Organic Frameworks
Catalytic selectivity Enzyme mimicking
1 Introduction
Nearly all new industrial processes in the chemical and
pharmaceutical industry are based on catalysis. In a society
where sustainability becomes increasingly important, a
chemists approach will be to develop more selective cat-
alysts that can minimize the use of raw materials and the
formation of byproducts. The most selective catalysts
known are natures own catalysts: enzymes. The dream of
many chemists, to be able to copy the functionality of
enzymes, is not new, but it is only in the last years that the
knowledge about enzyme structure and the mechanism in
enzyme functionality has reached the level where we can
see what the active site looks like and start to understand
how it works. But in order to make the dream come true,
man (chemist) must be able to make catalytic materials that
work in a similar manner as enzymes. We are unfortunately
still far from the goal of synthesizing structures in a
planned and controlled manner that are even close to the
complexity of the simplest enzymes, but we might be able
to copy some of natures ideas and implement this
K. P. Lillerud (&) U. Olsbye
Department of Chemistry, inGAP Center of Research-Based
Innovation, University of Oslo, Sem Selands vei 26, 0315 Oslo,
Norway
e-mail: k.p.lillerud@kjemi.uio.no
M. Tilset
Department of Chemistry, CTCC Centre for Theoretical and
Computational Chemistry, University of Oslo, Sem Selands vei
26, 0315 Oslo, Norway
1 3
Top Catal (2010) 53:859868
DOI 10.1007/s11244-010-9518-4
functionality into manmade materials. A direct copy of the
enzyme is probably not the optimal catalyst for an indus-
trial process. Nature is forced to operate within a very
limited temperature and pressure range; temperatures must
be typically between 0 and 50 C (rarely up to 80 C) and
partial pressures much below one atmosphere [1]. By
contrast, typical industrial process conditions are temper-
atures [120 C and partial pressures [1 atm. The tem-
perature has to be elevated to utilize the energy and an
increase in pressure will normally speed up the reaction.
Nature has elegant, selective processes but nature also is
too patientan industrial catalyst must have a higher
efciency. In discussions with colleagues in the industry,
some provocative ideas have been suggested: It should be
possible to make materials that perform even better than
enzymes! [2].
One approach might be to copy the chemical environ-
ment around the active site and to build this structural theme
into structures that are considerable more robust than the
fragile enzymes. This approach will be discussed further.
2 Enzyme Structure
One important step in understanding how enzymes work as
catalysts is to solve the crystal structure with a resolution that
allows a detailed description of the atoms that formthe active
site and the local environment around the active site in the
molecule. The rst enzyme structure was solved by Blake
et al. and published in Nature in 1965 [3]. The resolution was
2 A

and all details cannot be seen. The structure of the same

enzyme has nowbeen redetermined at 0.65 A

resolution [4],
a resolution that reveals essentially all necessary details.
Figure 1 illustrates this development in protein (enzyme)
crystallography that to a great extent is a result of the
development of synchrotrons giving brighter X-ray sources,
the technique of freezing the crystals in liquid nitrogen and
not least the development of the computer power with
software needed to solve structures with this complexity. For
further reading on the development of protein structure
solution and structure presentation, the web sites: http://
www.umass.edu/microbio/rasmol/1st_xtls.htm and http://
www.umass.edu/microbio/rasmol/history.htm are highly
recommended.
But of course, making crystals of the pure protein of
sufcient quality is difcult; there are therefore still many
interesting enzymes where the structure of the active site
has not been solved.
3 Enzyme Specicity, Active Site and Selectivity
The lock and key model that rationalizes enzyme spec-
icity was put forward by Fischer already in 1894 [5]. It is
based on a purely geometrical viewpoint that rationalizes
some of the superb stereospecicity demonstrated by
enzyme catalysts, but it fails to explain the stabilization of
the transition state achieved by the electrostatic eld inside
the cavity that embraces the reaction. Zeolites and related
oxide based microporous materials are manmade catalysts
that show a selectivity created by an analogous space
induced lock and key functionality [6, 7]. In some cases
the selectivity is so specic that it is claimed to be enzyme
like [8]. Figure 2 illustrates one of the complex organic
intermediates identied in the conversion of methanol to
olens: this intermediate has a perfect geometrical t to the
cavity, and transition states are also undoubtedly stabilized
by the electrostatic eld inside the zeolite cavities. This and
similar selective reactions have, however, mostly been
discovered by pure serendipity. The nature of the internal
cavities in these inorganic materials is too different from
what we see in enzymes to allow a transfer of the knowl-
edge from enzymatic catalysis to these materials. Another
limitation with zeolite type materials is the problem of
synthesis by design. Although synthesis of zeotype mate-
rials has been one of our main research topics for the past
Fig. 1 Illustration of the
development in protein
(enzyme) crystallography. Left
Original illustration of the rst
enzyme structure solved by
Blake et al. in Nature, 1965 [3].
The resolution is 2 A

and all
details cannot be seen. ( The
Nature publishing group, reprint
with permission). Right The
same enzyme at 0.65 A

resolution [4] a resolution that

reveals all details
860 Top Catal (2010) 53:859868
1 3
25 years we must admit that it is a huge challenge to make
a new material with designed properties.
An emerging new class of microporous materials
Metal Organic Frameworks (MOFs), on the other hand,
has properties that are promising in this respect. A signif-
icant portion of the internal surface of these materials is of
an organic nature and therefore more closely resembles the
surface that embraces the catalytic site in enzymes. So it is
possible to envisage that structural motifs from enzymes
might be recreated in these materials. Furthermore, as will
be discussed in more detail below, the possibility for cat-
alyst synthesis by design is much more feasible in MOF
materials when compared to the pure inorganic micropo-
rous materials.
Great structural and functional diversities are seen in the
active sites of enzymes, and we will choose as examples
enzymes where one or a few metals contribute to the cat-
alytic center. One example is the zinc, cobalt or even
cadmium atom that constitutes the center of the active site
in one of the most studied enzyme systems, Anhydrase [9].
Figure 3 is a simplied view of the zinc atom in a tetra-
hedral coordination environment, bonded to three nitrogen
based ligands and one water molecule. An organic hydro-
phobic cleft surrounds the site in this large enzyme mole-
cule. Figure 4 illustrates the surrounding cavity and
compares it with a cavity of comparable dimensions in the
MOF structure UiO-67 [10]. Incorporation of heteroatoms
and functional groups to the linker in the MOF will further
increase the similarity to enzyme internal surfaces.
4 MOF Construction and Flexibility
The essential concept of MOFs, connecting coordination
complexes by the use of ligands that bind to more than one
complex and thereby forming extended structures, is not
new [11], but it was the appearance of the new and spec-
tacular structures like MOF-5 [12], HKUST-1 [13] and
MIL-101 [14] that really attracted new researchers atten-
tion toward this class of nano(micro)porous materials.
Figure 5 illustrates the concept of extended MOF struc-
tures. A structural cornerstone might be formed either by a
single metal atom or, more commonly, by a metal cluster.
Another important advance in the development of the
MOF eld was the concept of isoreticular series of struc-
tures [15] pointing to the possibility of a more systematic
design and synthesis of these materials. There has been
an animated debate about the possibility of doing synthesis
by design within the MOF community [11]. One reason for
this controversy might be the dualistic nature of the MOF
materials; inorganic cornerstones connected with organic
linkers. A reliable prediction of the synthesis and resulting
Fig. 2 Illustration of the complex organicinorganic complex iden-
tied as the active site in the conversion of methanol to olens in H-
SAPO-34. The intermediate has a perfect geometrical t to the cavity
of the catalyst SAPO-34. Transition states are undoubtedly stabilized
by the electrostatic eld inside the zeolite cavity
Fig. 3 A simplied view of the active site in the anhydrase enzyme.
Zinc has a tetrahedral coordination with three nitrogen and one water
ligand. It is located in a well-dened organic hydrophobic cleft in the
large molecule
Top Catal (2010) 53:859868 861
1 3
structure of the inorganic part to a great extent still relies
on serendipity. By contrast, the structure of the organic
linkers are normally preserved at the relatively mild con-
ditions for MOF synthesis and this part of the structure can
therefore be controlled to a large extent. This dual nature is
the reason for the enormous exibility in these structures.
OKeefe et al. [16] have collected known coordination
complexes that are known to or might form cornerstones in
MOF structures. Figure 6 shows a small selection sorted by
coordination number. More complex inorganic structural
motifs like chains and sheets and even 3D inorganic
structures that are connected with organic ligands are also
known. Even for the structurally much simpler zeolites, the
number of possible structures is in principle innite. With
MOF structures is it possible to change the connection of
the inorganic cornerstone from two up to 12, and the
linkers might also have a variable connection, although in a
more limited range. This structural exibility is illustrated
in Fig. 7a, which addresses the variation in cornerstone
coordination, and in Fig. 7b, which gives examples of
structures with the same cornerstone but different linker
connectivity.
5 Introducing Catalytic Sites in MOF Structures
Until recently, most of the focus has been on the synthesis
of new MOF structures, but this is now slowly shifting
towards applications. Examples dealing mostly with
adsorption and separation appear frequently, but other
applications and among them catalysis also attract
increasing attention [17]. There are in principle two ways
of introducing catalytic active sites. One approach is to
incorporate an uncoordinated site at one of the metal atoms
in the inorganic cornerstone. Figure 8 illustrates this
Sodalite-type MOF structure with an expanded view of the
single Pd-atom cornerstone [18] at which Corma et al.
recently demonstrated catalytic activity [19]. An alterna-
tive approach that seems more appealing from the view-
point of mimicking enzymes is to build the active site into
the linker. Figure 9 illustrates this principle that has been
suggested by several groups [20, 21]. Figure 10 illustrates
ligands with catalytic centers.
Fig. 4 Left The cavity around
the active site in the anhydrase
enzyme. Right The surface in
the octahedral cage of the UiO-
67 MOF structure. The internal
surface of MOF based
nanoporous materials have more
similarities to enzyme surfaces,
compared to oxide based
surface of zeolites and related
oxide based microporous
materials, see Fig. 2
Fig. 5 Illustration of the MOF concept: a structural cornerstone
might be formed either by a single metal atom or, more commonly, by
a metal cluster which is connected by ligands that can form bonds to
more than one cornerstone. Bond energies are typically much larger
than what is found in coordination complexes Fig. 6 OKeeffe et al. have collected know coordination complexes
that are known to form or that might form cornerstones in MOF
structures. A small selection of these coordination complexes are
presented and sorted by coordination number, illustrating how nature
prefers high symmetry structures. 131 different metal clusters are
known today (2009)
862 Top Catal (2010) 53:859868
1 3
Fig. 7 The exibility in the construction of MOF structures are illustrated by a addressing how variation in cornerstone coordination creates new
structures and b examples of structures with the same cornerstone but different linker connectivity
Top Catal (2010) 53:859868 863
1 3
5.1 Example ReactionMethane Activation
One dream reaction that does not have any synthetic
industrial catalysts is the direct conversion of methane to
value-added functionalized products, but nature has
developed an enzyme for this process, known from the bath
bacteria [2226]. Our group has targeted this reaction with
platinum-based homogeneous catalysts long before the
structure of the enzyme was known. Figure 11 illustrates
the enzyme and the most active metal organic complex for
this reaction [27, 28]. Our work was inspired by the sem-
inal contributions from the Shilov group [29, 30], who
demonstrated that aqueous Pt(II) salts could activate alkane
CH bonds in aqueous acidic media. Periana later dem-
onstrated that Pt(II) salts supported by bidentate N-donor
ligands can catalytically functionalize methane to furnish
methyl bisulfate in fuming sulfuric acid [31], but the sys-
tem does not offer conversion rates that are even remotely
suitable for a large-scale industrial process [32]. A heter-
ogeneous catalyst with superior thermal stability is there-
fore highly desirable. The IRMOF-10 structure inspired us
to make a modied versions of this structure but with
bipyridine dicarboxylate linkers that could coordinate
Pt(II). Figure 12 illustrates such a structure. It is indeed
possible to make a structure like this but the chemical
stability of the MOF obtained is extremely poor. This
illustrates both one of the great advantages with MOF
materials and also an important disadvantage: It is possible
(but not necessarily easy) to go to the lab and make a
structure not too different from a designed material, but it
is our experience that MOFs are unfortunately often not
very robust, neither thermally nor chemically. In parallel
with our work it became apparent that the zinc cornerstones
in MOF-5 and related structures are very vulnerable to
humidity [33, 34]. We therefore directed our search
towards more robust MOF materials. Replacing zinc with
gadolinium resulted in a Pt-containing MOF with a much
higher chemical stability [3537]. Figure 13 shows the
Fig. 10 Ligands with catalytic centers
Fig. 11 Soft oxidation of methane to methanol is a reaction that has a
known enzyme catalyst (left). Among several homogenous catalysts,
the most active metal organic complex for soft activation of methane
is depicted (right). (Left Reproduced by permission of the Royal
Society of Chemistry)
Fig. 12 The IRMOF-10 structure and a modied versions of this
structure with bipyridine linkers for coordination of Pt(II)
Fig. 8 Illustration of the Sodalite-type MOF structure with an
expanded view of the single Pd-atom corner-stone [18]
Fig. 9 Creating catalytic activity in MOF structures by modication
of the linker. This principle has been suggested in parallel by several
groups [20, 21]
864 Top Catal (2010) 53:859868
1 3
asymmetric unit in this structure, with high temperature X-
ray diffraction data as an inset. The local platinum coor-
dination is as designed in the structure and the thermal
stability is very good, but with this system we were con-
fronted with a new general problem related to synthesis of
MOFs with active sites: This site will naturally coordinate
strongly both to the solvent used in the synthesis and to the
neighboring active site. The p-electrons on platinum tend
to coordinate to each other forming PtPt-stacking and
thereby blocking access to the active sites. Figure 14
illustrates this structure with nanoporous channels outlined
in blue. Guest molecules can access the structure but will
not reach the active sites.
A systematic search for alternative structures, through a
major part of the periodic table, was initiated both with
linker ligands that were uncoordinated to as well as pre-
coordinated to platinum. This resulted in a large number of
new and different MOF structures. Many of these exhibited
the familiar PtPt stacking, but several interesting new
structures without theses close contacts between the
potentially active sites were also found. One of the most
interesting new materials is a PtCu-MOF (Zeto et al., in
prep.). When working with this structure we realized that it
had several structural features that resemble the structure of
the methane monooxygenase enzyme [22]. The structure of
this enzyme has been solved at a resolution that reveals the
main features of the active site but still not all details, in
parallel with our synthetic work. Figure 15 shows the
molecular surface around the active site and the
Fig. 13 The asymmetric unit in
the PtGd-MOF structure, with
high temperature X-ray
diffraction data as an inset
Fig. 14 The nanoporous channels in the PtGd-MOF structure
outlined in blue. Guest molecules can access the structure but will
not reach the active sites
Fig. 15 The electron density map and the interpretation of the
coordination around the metals that are believed to be the active part
of the enzyme, as presented in [22]. ( The American Chemical
Society, reprinted with permission)
Top Catal (2010) 53:859868 865
1 3
interpretation of the coordination around the metals that are
believed to be the active part of the enzyme. Figure 16 is
an illustration of one cavity in our synthetic CuPt-MOF
this structure has motifs that are surprisingly similar to
parts of the enzyme structure.
The CuPt-MOF, which is structurally related to MOF-
505 [38] is sufciently thermally stable to allow removal of
most of the solvent. The measured BET surface is 650 m
2
/
g, but the calculated surface is above 1000 m
2
/g. Probably
there are remaining DMF molecules that stay in the
structure, possibly at the Pt sites with consequential inhi-
bition of catalytic activity. Renewed attempts to remove
the residual DMF by supercritical CO
2
extraction [39] is
underway. This example demonstrates that structures
resembling small parts of enzyme structures can be syn-
thesized, but we have to admit that this structure was found
by serendipity. However, in the example below we will
describe a successful planned synthesis.
5.2 Example ReactionAnhydrase
One of the most studied and also most important enzyme
systems is the carbonic anhydrase. This enzyme is vital for
all living organisms from primitive plants to mammals.
Nature has developed multiple modications of this
enzyme, and in mammals alone 14 modications are
known [9]. In addition to its crucial importance for all
living organisms that adsorb or expel CO
2
, the current
focus on climate change and CO
2
capture technologies has
created an industrial interest in anhydrase. Patents have
been led that suggest large scale use of anhydrase in CO
2
capture [40].
Zinc is the active metal for the majority of anhydrase
enzymes, but there exist modications of anhydrase with
cobalt and even cadmium [41] as the catalytically active
metal.
The reactive site in the enzyme is assumed to be a ZnOH
species (or other metals, i.e., Co, Cd). The proposed cata-
lytic cycle contains the steps of
reaction of ZnOH and CO
2
to form a bicarbonate
complex;
ejection of the bicarbonate ion and formation of a
Zn(H
2
O) complex;
proton dissociation to give a ZnOH moiety and a
protonated histidine group close to the Zn center.
Several attempts to mimic the active site of this enzyme
with coordination chemistry based on model Zn coordina-
tion complexes have been pursued, albeit with no success
in mimicking the active Zn site in carbonic anhydrase [42,
43]. The active site is proposed to contain a Zn atom in a
tetrahedral coordination sphere connected to histidine
ligands. Model studies [44, 45] have so far activated
CO
2
, but the process stopped at the bicarbonate complex
(product inhibition).
Figure 17 is an illustration of the Zn-complex from Ref.
[39] with water as the fourth, too strongly bound, ligand.
Thus, apparently the activation of water is an important
step in the proposed catalytic cycle. As a consequence the
pK
a
of the conjugate acid coordinated water molecule has
been the subject of some discussion [46]. In Zn containing
carbonic anhydrase the pK
a
of the water molecule has been
reported to be in the range of 6.97.7, whereas the pK
a
range quoted for [Zn(H
2
O)
6
]
2?
is two units higher. This
has led to a proposal that the low pK
a
value for the coor-
dinated water molecule in carbonic anhydrase is in part a
consequence of the hydrophobic environment around the
active protein site. According to the authors of Ref. [39],
Fig. 16 A new CuPt-MOF from UiO showing structural units that
are surprisingly similar to the active site in the methane monooxy-
genase enzyme
Fig. 17 The Zn-complex from Ref. [39] with water as the fourth, too
strongly bound, ligand
866 Top Catal (2010) 53:859868
1 3
Structural studies show that the zinc atom in Zn(II) car-
bonic anhydrase is situated at the bottom of a cleft, lined
with hydrophobic groups in the protein molecule. It has
been postulated that this local hydrophobic environment is
largely responsible for the decreased pK
a
of the coordi-
nated water molecule.
It is therefore necessary to mimic both the metal site and
the local environment with the right hydrophobic character.
This can probably be done by coordinating the active metal
inside a porous solid that has a hydrophobic internal sur-
face. Cobalt coordinated to a bipyridine linker in a modi-
ed UiO-67 may well be a suitable candidate. Figure 18
illustrates such a structure with cobalt in this coordination
environment.
This MOF structure has also the property that it can
reversibly adsorb and desorb water at the Zr
6
-cornerstone.
This phenomenon utilizes the unusual property of zirco-
nium that it is stable both in a seven- and eight-coordina-
tion mode. This site, offering variable hydrophobic
character depending on the coordination, is located next to
the metal site like the histidine ligand in the enzyme.
6 Conclusion and Outlook
Approaching enzyme selectivity while maintaining indus-
trial type catalysts activity and robustness must be among
the ultimate goals for catalyst development in the twenty-
rst century. The contributions to these proceedings from
Somorjai and Li address how advances in nanotechnology
enable the control of catalytically active structures on
surfaces. This contribution addresses the synthesis of
nanostructures inside nanopores. Enzyme specicity is a
result of the synergy between the active site itself and the
shaping of the environment around this site.
The overall structure of enzymes is far too complex to
be copied as manmade materials in the foreseeable future,
but several groups, with some examples discussed above,
have demonstrated that small fragments of structural motifs
revealed by high resolution X-ray structure determination
of enzyme structures can be incorporated into MOF
structures. This allows recreation of catalytic sites as well
as their local environments. We have thereby moved a
signicant step further in the direction of copying, not yet
the catalytic activity, but the idea or structural motives
from enzymes into manmade materials. These materials are
much simpler and more regular compared to enzymes, but
this is also a part of our goal since we aim at making more
stable materials compared to the enzymes.
There is, however, much more to enzyme specicities
than their static structures. An important contribution to
both activity and selectivity of enzymes is their structural
exibility and their dynamic behavior [47]. These are
properties that are much more challenging to transfer into
simpler, more regular, materials. Higher thermal stability
will inevitably also result in more rigid structures. A per-
fect transfer of the catalytic center with its local environ-
ment unaltered might therefore still not be sufcient to
recreate the catalytic properties.
Acknowledgments Elin Grahn, O

rebro University is acknowledged

for her help with enzyme structures. This work was supported by The
Research Council of Norway project no: 158552/431 and the Euro-
pean Commission (NMP4-CT-2006-033335 MOFCAT).
References
1. Benkovic SJ, Hammes-Schiffer S (2003) Science 301:1196
2. Christensen CH (2008) Private communication
3. Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma
VR (1965) Nature 206:757
4. Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z (1254) Acta
Crystallogr D Biol Crystallogr D63:1254
5. Fischer E (1894) Ber Deutsch Chem Ges 27:3189
6. Arstad B, Kolboe S (2001) J Am Chem Soc 123:8137
7. Svelle S, Olsbye U, Lillerud K-P, Kolboe S, Bjorgen M (2006) J
Am Chem Soc 128:5618
8. Boronat M, Martinez-Sanchez C, Law D, Corma A (2008) J Am
Chem Soc 130:16316
9. Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC (2000)
Biochemistry 39:9222
10. Hazovic Cavka J, Jakobsen S, Olsbye U, Guillou N, Lamberti C,
Bordiga S, Lillerud KP (2008) J Am Chem Soc 130:13850
11. Ferey G (2008) Chem Soc Rev 37:191
12. Li H, Eddaoudi M, OKeeffe M, Yaghi M (1999) Nature 402:276
Fig. 18 Top The isoreticular series of Zr-MOFs, UiO-66-68. Bottom
Cobalt coordinated to a bipyridine linker in a modied UiO-67
Top Catal (2010) 53:859868 867
1 3
13. Chui SSY, Lo SMF, Charmant JPH, Orpen AG, Williams ID
(1999) Science 283:1148
14. Ferey G, Mellot-Draznieks C, Serre C, Millange F, Dutour J,
Surble S, Margiolaki I (2005) Science 309:2040
15. Eddaoudi M, Kim J, Rosi N, Vodak D, Wachter J, OKeeffe M,
Yaghi OM (2002) Science 295:469
16. Tranchemontagne DJ, Mendoza-Cortes JL, OKeeffe M, Yaghi
OM (2009) Chem Soc Rev 38:1257
17. Lee JY, Farha OK, Roberts J, Scheidt KA, Nguyen SBT, Hupp JT
(2009) Chem Soc Rev 38:1450
18. Navarro JAR, Barea E, Salas JM, Masciocchi N, Galli S, Sironi
A, Ania CO, Parra JB (2006) Inorg Chem 45:2397
19. Llabres i Xamena FX, Abad A, Corma A, Garcia H (2007) J Catal
250:294
20. Ma L, Abney C, Lin W (2009) Chem Soc Rev 38:1248
21. Lillerud K-P, Tilset M, Olsbye U, Szeto KC, Bjoergen M, Kon-
gshaug KO, Bordiga S, Hazovic J, Krivokapic A, Jakobsen S
(2007) PCT Int Appl WO 2007007113 A2 20070118
22. Balasubramanian R, Rosenzweig AC (2007) Acc Chem Res
40:573
23. Hakemian AS, Rosenzweig AC (2007) Annu Rev Biochem
76:223
24. Ukaegbu UE, Rosenzweig AC (2009) Biochemistry 48:2207
25. Sommerhalter M, Lieberman RL, Rosenzweig AC (2005) Inorg
Chem 44:770
26. Lieberman RL, Rosenzweig AC (2005) Nature 434:177
27. Johansson L, Ryan OB, Romming C, Tilset M (2001) J Am Chem
Soc 123:6579
28. Johansson L, Ryan OB, Tilset M (1999) J Am Chem Soc
121:1974
29. Goldshleger NF, Tyabin MB, Shilov AE, Shteinman AA (1969)
Zh Fiz Khim 43:2174
30. Shilov AE, Shulpin GB (1997) Chem Rev 97:2879
31. Periana RA, Taube DJ, Gamble S, Taube H, Satoh T, Fujii H
(1998) Science 280:560
32. Ahlquist M, Nielsen RJ, Periana RA, Goddard WA III (2009)
J Am Chem Soc 131:17110
33. Schroeck K, Schroeder F, Heyden M, Fischer RA, Havenith M
(2008) Phys Chem Chem Phys 10:4732
34. Kaye SS, Dailly A, Yaghi OM, Long JR (2007) J Am Chem Soc
129:14176
35. Szeto KC, Kongshaug KO, Jakobsen S, Tilset M, Lillerud KP
(2008) Dalton Trans 2054
36. Szeto KC, Lillerud KP, Tilset M, Bjorgen M, Prestipino C,
Zecchina A, Lamberti C, Bordiga S (2006) J Phys Chem B
110:21509
37. Szeto KC, Prestipino C, Lamberti C, Zecchina A, Bordiga S,
Bjorgen M, Tilset M, Lillerud KP (2007) Chem Mater 19:211
38. Millward AR, Yaghi OM (2005) J Am Chem Soc 127:17998
39. Nelson AP, Farha OK, Mulfort KL, Hupp JT (2009) J Am Chem
Soc 131:458
40. Dutil F, Villeneuve C (2003) US Pat Appl Publ US 2003143719
A1 20030731
41. Xu Y, Feng L, Jeffrey PD, Shi Y, Morel FMM (2008) Nature
452:56
42. Vahrenkamp H (2007) Dalton Trans 4751
43. Parkin G (2004) Chem Rev 104:699
44. Brombacher H, Vahrenkamp H (2004) Inorg Chem 43:6042
45. Rombach M, Brombacher H, Vahrenkamp H (2002) Eur J Inorg
Chem 1:153
46. Coates JH, Gentle GJ, Lincoln SF (1974) Nature 249:773
47. Lim K, Read RJ, Chen CCH, Tempczyk A, Wei M, Ye D, Wu C,
Dunaway-Mariano D, Herzberg O (2007) Biochemistry 46:14845
868 Top Catal (2010) 53:859868
1 3