Chemistry - A European Journal
10.1002/chem.202100680
COMMUNICATION
we demonstrated the benzene containing small molecules could
dock in close proximity to the heme group of OleT (Figure 1B, 1C,
S2), which led to the shifts of heme spectra (Figure 2A 2B and
Keywords: cytochrome • P450 OleT • biocatalysis • enzyme-
small molecule interaction • 1-alkene • decarboxylase
2 2
Figure S3). Our results showed that the enzyme could use H O
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increasing concentration of H , OleTSA showed decreased
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.[20] The
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concentration. For example, when 0.2 mM of H was used,
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2
oxidative stress releasing involved mechanism. To confirm this
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generate H
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used, the small molecule’ enhanced effect on the enzyme activity
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In summary, a panel of small molecules has been used to
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hypothesize that the small molecules could reside in the enzyme
active site and serve as a new type of OleT enzyme modulator.
We postulate that the origin of the enhancement is from the
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2
O
2
can be used more
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efficiently with reduced enzyme toxicity. Further mechanistic
investigation, especially on the enzyme-small molecule-substrate
complex structure data, is necessary to better understand the
system. Our work sheds the light to the development of small
molecular activators to increase OleT catalytic activity, which
could be potentially used for future olefin-production applications.
[
[
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Acknowledgements
QW and LZ acknowledge the partial financial support from the
NSF and SC EPSCoR/IDeA Program under NSF Award #OIA-
462–466.
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J. Biol. Chem. 2017, 292, 5128–5143.
1655740. The views, perspective, and content do not necessarily
represent the official views of the SC EPSCoR/IDeA Program nor
those of the NSF. DM acknowledges support (201806310084)
from the State Scholarship Fund of the China Scholarship Council.
All authors thank Professor Thomas M. Makris for providing
OleTSA enzyme and the plasmids. We also thank Olivia Manley,
Suman Das and Dr. Jose A. Amaya from Makris Group for their
help on the protein purification and analysis. We also
acknowledge support from the staffs at the Mass Spectrometry at
the University of South Carolina.
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