Issue 32, 2022
From the journal:

Chemical Science

Tuning through-space interactions via the secondary coordination sphere of an artificial metalloenzyme leads to enhanced Rh(iii)-catalysis†

Isra S. Hassan,‡a   Jack T. Fuller,‡b   Vanessa N. Dippon,a   Angeline N. Ta,c   Michael W. Danneman,a   Brian R. McNaughton,§*c   Anastassia N. Alexandrova ORCID logo *b  and  Tomislav Rovis ORCID logo *a  

* Corresponding authors

a Department of Chemistry, Columbia University, New York, NY, USA
E-mail: tr2504@columbia.edu

b Department of Chemistry & Biochemistry, University of California Los Angeles, Los Angeles, CA, USA
E-mail: ana@chem.ucla.edu

c Department of Chemistry, Colorado State University, Fort Collins, CO, USA
E-mail: bmcnaughton@desu.edu

Abstract

We report computationally-guided protein engineering of monomeric streptavidin Rh(III) artificial metalloenzyme to enhance catalysis of the enantioselective coupling of acrylamide hydroxamate esters and styrenes. Increased TON correlates with calculated distances between the Rh(III) metal and surrounding residues, underscoring an artificial metalloenzyme's propensity for additional control in metal-catalyzed transformations by through-space interactions.

Graphical abstract: Tuning through-space interactions via the secondary coordination sphere of an artificial metalloenzyme leads to enhanced Rh(iii)-catalysis

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Article information

DOI
https://doi.org/10.1039/D2SC03674F
Article type
Edge Article
Submitted
30 Jun 2022
Accepted
28 Jul 2022
First published
29 Jul 2022
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2022,13, 9220-9224

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Tuning through-space interactions via the secondary coordination sphere of an artificial metalloenzyme leads to enhanced Rh(III)-catalysis

I. S. Hassan, J. T. Fuller, Vanessa N. Dippon, A. N. Ta, M. W. Danneman, B. R. McNaughton, A. N. Alexandrova and T. Rovis, Chem. Sci., 2022, 13, 9220 DOI: 10.1039/D2SC03674F

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