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Table 1 Kinetic parameters for the (Z)-diacid catalyzed hydrolysis of
4-nitrophenyl-b-D-glucopyranoside at pH 5.8 and 25 1Cb
Soc. Rev., 2011, 40, 4422; (c) C. Renner and L. Morder, ChemBioChem,
¨
2006, 7, 868; (d) B. Reisinger, N. Kuzmanovic, P. Loffler, R. Merkl,
¨
B. Konig and R. Sterner, Angew. Chem., Int. Ed., 2014, 53, 595;
a
(e) I. Tochitsky, A. Polosukhina, V. E. Degtyar, N. Gallerani, C. M.
Smith, A. Friedman, R. N. Van Gelder, D. Trauner, D. Kaufer and
R. H. Kramer, Neuron, 2014, 81, 800.
2 (a) C. Brieke, F. Rohrbach, A. Gottschalk, G. Mayer and A. Heckel,
Angew. Chem., Int. Ed., 2012, 51, 8446; (b) K. Li, Y. Xiang, X. Wang,
J. Li, R. Hu, A. Tong and B. Z. Tang, J. Am. Chem. Soc., 2014, 136, 1643.
3 (a) W. A. Velema, W. Szymanski and B. L. Feringa, J. Am. Chem. Soc.,
2014, 136, 2178; (b) W. A. Velema, J. P. van der Berg, M. J. Hansen,
W. Szymanski, A. J. M. Driessen and B. L. Feringa, Nat. Chem., 2013,
5, 924.
kcat
knon
KM
(mM)
kcat/KM
(minꢁ1
)
(minꢁ1
)
kcat/knon
(mMꢁ1 minꢁ1
)
2.4 ꢂ 103
4.8 ꢂ 10ꢁ4
5.0 ꢂ 106
2.6
9.2 ꢂ 102
a
b
knon = knoncatalyzed
.
With the (E)-isomer the rate enhancement at this
pH was essentially the same as the background reaction.
4 C. Renner and L. Morder, ChemBioChem, 2006, 7, 868.
5 (a) N. Muranaka, T. Hohsaka and M. Sisido, FEBS Lett., 2002,
510, 10; (b) K. Nakayama, M. Endo and T. P. Majima, Chem.
Commun., 2004, 2386.
6 (a) Y. Norikane and N. Tamaoki, Org. Lett., 2004, 6, 2595;
(b) H. Murakami, A. Kawabuchi, K. Kotoo, M. Kunitake and
N. Nakashima, J. Am. Chem. Soc., 1997, 119, 7605; (c) T. Muraoka,
K. Kinbara and T. Aida, Nature, 2006, 440, 512.
7 For example: (a) Y. Oka and N. Tamaoki, Inorg. Chem., 2010,
49, 4765; (b) A. Momotake and T. Arai, Tetrahedron Lett., 2003,
44, 7277; (c) C. J. Roxburgh and P. G. Sammes, Eur. J. Org. Chem.,
2006, 1050; (d) I. Takahashi, Y. Honda and S. Hirota, Angew. Chem.,
Int. Ed., 2009, 48, 6065.
Fig. 6 Proposed catalytic mechanism of the (Z)-diacid with the substrate
with 4-nitrophenyl-b-D-glucopyranoside; note the presence of the water
molecule.
8 (a) Y. Wang, F. Bie and H. Jiang, Org. Lett., 2010, 12, 3630; (b) Y. Hua
and A. H. Flood, J. Am. Chem. Soc., 2010, 132, 12838.
it was observed that two molecules of water fit between the
substrate and the azobenzene molecules. It can thus be speculated
that the phenolic oxygen of the 4-nitrophenyl group which is in
close proximity to the carboxylic acid group of the (Z)-azobenzene is
protonated by the acid (Fig. 6). The carboxylate unit deprotonates a
molecule of water which in turn deprotonates the neighboring
water molecule that attacks the carbon bearing the 4-nitrophenyl
leaving group.
The catalytic action of the enzyme mimic can be switched
reversibly with light by toggling the (E)–(Z) isomerisation as shown
in Fig. S7, ESI.‡ The thermal stability of the (Z)-form has been
investigated (Fig. S8 and S9, ESI‡) and the activation parameters for
the thermal reaction are provided in Table S1, ESI.‡
The (E)-isomer of the azobenzene-3,30-dicarboxylic acid photo-
switch shows a single pKa for the deprotonation of the acidic
protons, whereas the (Z)-isomer shows two distinct pKa values
indicating a stepwise loss of the protons from the acid. In the pH
range of 4.7 to 6.5, the (Z)-isomer exists in the acid–conjugate base
form where the –COOH and the –COOꢁ groups can act as a general
acid and a general base respectively. The catalytic activity of the
(Z)-isomer as a glycosidase mimic at pH 5.8 was found to be highly
efficient with a rate enhancement of six orders in magnitude
compared to the background. This is the first example of a
photo-controlled glycosidase activity with an enzyme mimic.
We thank CSIR for support (grant # 01(2717)/13/EMR-II) and
UGC, New Delhi, for a Fellowship to MS VSRK is supported by
an Int. PhD fellowship from IISER Kolkata.
9 (a) G. H. Clever, S. Tashiro and M. Shionoya, J. Am. Chem. Soc., 2010,
132, 9973; (b) M. Liu, X. Yan, M. Hu, X. Chen, M. Zhang, B. Zheng,
X. Hu, S. Shao and F. Huang, Org. Lett., 2010, 12, 2558; (c) J. Cao,
J. B. Guo, P. F. Li and C. F. Chen, J. Org. Chem., 2011, 76, 1644;
(d) C. Dugave and L. Demange, Chem. Rev., 2003, 103, 2475.
10 S. H. Kawai, S. L. Gilat and J.-M. Lehn, Eur. J. Org. Chem., 1999, 2359.
11 Y. Odo, K. Matsuda and M. Irie, Chem. – Eur. J., 2006, 12, 4283.
12 S. Kobatake and Y. Terakawa, Chem. Commun., 2007, 1698.
13 J. Massaad, J.-C. Micheau, C. Coudret, R. Sanchez, G. Guirado and
S. Delbaere, Chem. – Eur. J., 2012, 18, 6568.
14 (a) F. Wu¨rthner and J. Rebek, J. Chem. Soc., Perkin Trans. 2, 1995,
1727; (b) M. V. Peters, R. S. Stoll, A. Ku¨hn and S. Hecht, Angew. Chem.,
Int. Ed., 2008, 47, 5968; (c) D. Sud, T. B. Norsten and N. R. Branda,
Angew. Chem., Int. Ed., 2005, 44, 2019For a comprehensive review on
reactions controlled by photoswitchable systems see: (d) R. S. Stoll
and S. Hecht, Angew. Chem., Int. Ed., 2010, 49, 5054.
15 (a) R. Breslow, Chem. Soc. Rev., 1972, 1, 553; (b) R. Breslow and
S. D. Dong, Chem. Rev., 1998, 98, 1997; (c) A. J. Kirby, Angew. Chem.,
Int. Ed. Engl., 1994, 33, 551.
16 Artificial Enzymes, ed. R. Breslow, Wiley-VCH, Weinheim, Germany,
2005.
17 (a) D. Piszkiewicz and T. C. Bruice, J. Am. Chem. Soc., 1968, 90, 2156;
(b) E. Anderson and T. H. Fife, J. Am. Chem. Soc., 1973, 95, 6437;
(c) K. E. S. Dean and A. J. Kirby, J. Chem. Soc., Perkin Trans. 2, 2002,
428.
18 (a) Y. Zhou, C. M. Pedersen and M. Bols, Tetrahedron Lett., 2013,
54, 2458; (b) F. Ortega-Caballero, C. Rousseau, B. Christensen,
T. E. Petersen and M. Bols, J. Am. Chem. Soc., 2005, 127, 3238;
(c) J. Bjerre, E. H. Nielsen and M. Bols, Eur. J. Org. Chem., 2008, 745;
(d) F. Ortega-Caballero and M. Bols, Can. J. Chem., 2006, 84, 650;
¨
(e) E. Lindback, Y. Zhou, C. M. Pedersen and M. Bols, Eur. J. Org.
Chem., 2012, 5366.
19 (a) Q.-H. Fan, S. Striegler, R. G. Langston and J. D. Barnett, Org.
Biomol. Chem., 2014, 12, 2792; (b) S. Striegler and M. G. Gichinga,
Chem. Commun., 2008, 5930; (c) S. Striegler, M. G. Gichinga and
M. Dittel, Org. Lett., 2008, 10, 241.
20 (a) J. McCarter and S. G. Withers, Curr. Opin. Struct. Biol., 1994,
4, 885; (b) D. L. Zechel and S. G. Withers, Acc. Chem. Res., 2000,
33, 11.
Notes and references
1 (a) J. Levitz, C. Pantoja, B. Gaub, H. Janovjak, A. Reiner, A. Hoagland, 21 A. J. Kirby and F. Hollfelder, From Enzyme Models to Model Enzymes,
D. Schoppik, B. Kane, P. Stawski, A. F. Schier, D. Trauner and E. Y. Isacoff, 2009.
Nat. Neurosci., 2013, 16, 507; (b) A. A. Beharry and G. A. Woolley, Chem. 22 M. A. Thompson, ArgusLab 4.0, Planaria Software LLC, Seattle.
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