Tuning through-space interactions <i>via</i> the secondary coordination sphere of an artificial metalloenzyme leads to enhanced Rh(<scp>iii</scp>)-catalysis-Reference-Cited by-同舟云学术

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

Published:2022 Issue:32 Volume:13 Page:9220-9224
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Hassan Isra S.¹,Fuller Jack T.²,Dippon Vanessa N.¹,Ta Angeline N.³,Danneman Michael W.¹,McNaughton Brian R.³,Alexandrova Anastassia N.²^ORCID,Rovis Tomislav¹^ORCID

Affiliation:

1. Department of Chemistry, Columbia University, New York, NY, 10027, USA

2. Department of Chemistry & Biochemistry, University of California Los Angeles, Los Angeles, CA, 90095, USA

3. Department of Chemistry, Colorado State University, Fort Collins, CO, 80523, USA

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.

Funder

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D2SC03674F

Reference37 articles.

1. Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

2. Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium(I) moiety

3. Artificial Metalloenzymes: (Strept)avidin as Host for Enantioselective Hydrogenation by Achiral Biotinylated Rhodium−Diphosphine Complexes