Organic & Biomolecular Chemistry
Communication
tion was performed at the 0.05 mmol scale for 2a with
0.37 mol% loading of a catalyst under neutral conditions [PBS
buffer (pH 7.4)/CH3CN = 10 : 1]. Pleasingly, product 3a was iso-
lated in 49% yield, corresponding to ca. 13 300 TON. Although
asymmetric induction by this wild-type protein was very
limited (5% ee), it holds promise to exhibit high enantio-
selectivity with other hemoproteins and by means of the state-
of-the-art directed evolution.20
4 For recent references, see: (a) S. C. Hammer, G. Kubik,
E. Watkins, S. Huang, H. Minges and F. H. Arnold, Science,
2017, 358, 215–218; (b) C. K. Prier, R. K. Zhang,
A. R. Buller, S. Brinkmann-Chen and F. H. Arnold, Nat.
Chem., 2017, 9, 629–634; (c) D. A. Vargas, A. Tinoco,
V. Tyagi and R. Fasan, Angew. Chem., Int. Ed., 2018, 57,
9911–9915; (d) K. Chen, S. Q. Zhang, O. F. Brandenberg,
X. Hong and F. H. Arnold, J. Am. Chem. Soc., 2018, 140,
16402–16407; (e) R. Fasan, D. Vargas, R. Khade and
Y. Zhang, Angew. Chem., Int. Ed., 2019, 58, 10148–10152;
(f) I. Cho, Z. Jia and F. H. Arnold, Science, 2019, 364, 575–
578; (g) J. Zhang, X. Huang, R. K. Zhang and F. H. Arnold,
J. Am. Chem. Soc., 2019, 141, 9798–9802; (h) R. K. Zhang,
K. Chen, X. Huang, L. Wohlschlager, H. Renata and
F. H. Arnold, Nature, 2019, 565, 67–72.
5 (a) X. Xu, C. Li, Z. Tao and Y. Pan, Adv. Synth. Catal., 2015,
357, 3341–3345; (b) X. Xu, C. Li, Z. Tao and Y. Pan, Green
Chem., 2017, 19, 1245–1249; (c) X. Xu, C. Li, M. Xiong,
Z. Tao and Y. Pan, Chem. Commun., 2017, 53, 6219–6222.
6 (a) P. Böhm and H. Gröger, ChemCatChem, 2015, 7, 22–28;
(b) R. A. Baglia, J. P. T. Zaragoza and D. P. Goldberg, Chem.
Rev., 2017, 117, 13320–13352.
Conclusions
In summary, we have reported the catalytic oxidative phenol–
indole [3 + 2] coupling reaction in aqueous media for the first
time. This system is valuable not only for providing biologi-
cally significant benzofuroindolines but also for showing the
potential of naturally abundant hemin for oxidative phenol
coupling reaction and Lewis acid catalysis. Provided a central
function of hemin for the family of cytochromes, P450
enzymes, the present study is anticipated to stimulate further
exploration of hemin catalysis and, in turn, push the boundary
of classic heme biocatalysis.
7 (a) A. W. G. Burgett, Q. L. Li, Q. Wei and P. G. Harran,
Angew. Chem., Int. Ed., 2003, 42, 4961–4966;
(b) K. C. Nicolaou, U. Majumder, S. P. Roche and D.
Y.-K. Chen, Angew. Chem., Int. Ed., 2007, 46, 4715–4718;
(c) T. S. Kam, S. J. Tan, S. W. Ng and K. Komiyama, Org.
Lett., 2008, 10, 3749–3752; (d) Y. Hirasawa, H. Arai,
A. Rahman, I. Kusumawati, N. C. Zaini, O. Shirota and
H. Morita, Tetrahedron, 2013, 69, 10869–10875.
Conflicts of interest
The authors declare no competing financial interest.
Acknowledgements
8 (a) W. Tian, L. R. Chennamaneni, T. Suzuki and D.
Y.-K. Chen, Eur. J. Org. Chem., 2011, 2011, 1027–1031;
(b) L. H. Liao, C. Shu, M. Zhang, Y. Liao, X. Hu, Y. Zhang,
Z. Wu, W. Yuan and X. Zhang, Angew. Chem., Int. Ed., 2014,
53, 10471–10475; (c) H. Ding, P. L. DeRoy, C. Perreault,
A. Larive, A. Siddiqui, C. G. Caldwell, S. Harran and
P. G. Harran, Angew. Chem., Int. Ed., 2015, 54, 4818–4822;
(d) D. Lachkar, N. Denizot, G. Bernadat, K. Ahamada,
M. A. Beniddir, V. Dumontet, J. F. Gallard, R. Guillot,
K. Leblanc, E. O. N′nang, V. Turpin, C. Kouklovsky,
E. Poupon, L. Evanno and G. Vincent, Nat. Chem., 2017, 9,
793–798; (e) Q. J. Liu, J. Zhu, X. Y. Song, L. Wang,
S. R. Wang and Y. Tang, Angew. Chem., Int. Ed., 2018, 57,
3810–3814; (f) L. Zhang, J. Hu, R. Xu, S. Pan, X. Zeng and
G. Zhong, Adv. Synth. Catal., 2019, 361, DOI: 10.1002/
adsc.201901035.
9 M. G. Peter and U. Wollenberger, Phenol-oxidizing
Enzymes: Mechanisms and Applications in Biosensors, in
Frontiers in Biosensorics I. Birkhäuser, Basel, 1997, 63–82.
10 For uses of iron porphyrin complexes in environmental
phenol degradation, see: (a) J. Yu, K. E. Taylor, H. Zou,
N. Biswas and J. K. Bewtra, Environ. Sci. Technol., 1994, 28,
2154–2160; (b) U. Khan and J. A. Nicell, J. Chem. Technol.
Biotechnol., 2007, 82, 818–830.
We thank the National Natural Science Foundation of China
(No. 21602067, 31770866), the Huazhong University of Science
and Technology (No. 2016YXMS183, 2018JYCXJJ040) and the
Science, Technology and Innovation Commission of Shenzhen
Municipality (JCYJ20180305180832515) for financial support.
We are also grateful to the Analytical and Testing Centre of
HUST, the Analytical and Testing Centre of School of
Chemistry and Chemical Engineering (HUST) for providing
access to their facilities. We thank Professor Guo-Chuan Yin
for insightful discussion.
Notes and references
1 I. Bertini and A. Sigel, Handbook on Metalloproteins. CRC
Press, 2001.
2 (a) I. G. Denisov, T. M. Makris, S. G. Sligar and
I. Schlichting, Chem. Rev., 2005, 105, 2253–2278;
(b) T. L. Poulos, Chem. Rev., 2014, 114, 3919–3962.
3 For leading reviews, see: (a) R. Fasan, ACS Catal., 2012, 2,
647–666; (b) F. H. Arnold, Angew. Chem., Int. Ed., 2018, 57,
4143–4148; (c) R. K. Zhang, X. Huang and F. H. Arnold,
Curr. Opin. Chem. Biol., 2019, 49, 67–75; (d) U. Markel,
D. F. Sauer, J. Schiffels, J. Okuda and U. Schwaneberg, 11 Q. Yu, Y. Fu, J. Huang, J. Qin, H. Zuo, Y. Wu and F. Zhong,
Angew. Chem., Int. Ed., 2019, 58, 4454–4464.
ACS Catal., 2019, 9, 7285.
This journal is © The Royal Society of Chemistry 2019
Org. Biomol. Chem., 2019, 17, 9994–9998 | 9997