Chimeric streptavidins as host proteins for artificial metalloenzymes

Michela M. Pellizzoni; Fabian Schwizer; Christopher W. Wood; Valerio Sabatino; Yoann Cotelle; Stefan Matile; Derek N. Woolfson; Thomas R. Ward

doi:10.1021/acscatal.7b03773

Chimeric streptavidins as host proteins for artificial metalloenzymes

Michela M. Pellizzoni, Fabian Schwizer, Christopher W. Wood, Valerio Sabatino, Yoann Cotelle, Stefan Matile, Derek N. Woolfson, Thomas R. Ward^*

^*Corresponding author for this work

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial metalloenzymes (ArM) for asymmetric transfer hydrogenation, ring-closing metathesis and anion catalysis. The additional second coordination sphere elements significantly influence both the activity and the selectivity of the resulting hybrid catalysts. These findings lead to the identification of propitious chimeric streptavidins for future directed evolution efforts of artificial metalloenzymes.

Original language	English
Pages (from-to)	1476-1484
Number of pages	9
Journal	ACS Catalysis
Volume	8
Issue number	2
DOIs	https://doi.org/10.1021/acscatal.7b03773
Publication status	Published - 2 Feb 2018

Keywords / Materials (for Non-textual outputs)

anion π catalysis
artificial metalloenzyme
chimeric protein
protein design
protein engineering
ring-closing metathesis
transfer hydrogenation

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10.1021/acscatal.7b03773

WardEtal2019ChimericStreptavidinsAsHostProteinsForArtificialMetalloenzymesAccepted author manuscript, 1.23 MB

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title = "Chimeric streptavidins as host proteins for artificial metalloenzymes",

abstract = "The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial metalloenzymes (ArM) for asymmetric transfer hydrogenation, ring-closing metathesis and anion catalysis. The additional second coordination sphere elements significantly influence both the activity and the selectivity of the resulting hybrid catalysts. These findings lead to the identification of propitious chimeric streptavidins for future directed evolution efforts of artificial metalloenzymes.",

keywords = "anion π catalysis, artificial metalloenzyme, chimeric protein, protein design, protein engineering, ring-closing metathesis, transfer hydrogenation",

author = "Pellizzoni, {Michela M.} and Fabian Schwizer and Wood, {Christopher W.} and Valerio Sabatino and Yoann Cotelle and Stefan Matile and Woolfson, {Derek N.} and Ward, {Thomas R.}",

year = "2018",

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day = "2",

doi = "10.1021/acscatal.7b03773",

language = "English",

volume = "8",

pages = "1476--1484",

journal = "ACS Catalysis",

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TY - JOUR

T1 - Chimeric streptavidins as host proteins for artificial metalloenzymes

AU - Pellizzoni, Michela M.

AU - Schwizer, Fabian

AU - Wood, Christopher W.

AU - Sabatino, Valerio

AU - Cotelle, Yoann

AU - Matile, Stefan

AU - Woolfson, Derek N.

AU - Ward, Thomas R.

PY - 2018/2/2

Y1 - 2018/2/2

N2 - The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial metalloenzymes (ArM) for asymmetric transfer hydrogenation, ring-closing metathesis and anion catalysis. The additional second coordination sphere elements significantly influence both the activity and the selectivity of the resulting hybrid catalysts. These findings lead to the identification of propitious chimeric streptavidins for future directed evolution efforts of artificial metalloenzymes.

AB - The streptavidin scaffold was expanded with well-structured naturally occurring motifs. These chimeric scaffolds were tested as hosts for biotinylated catalysts as artificial metalloenzymes (ArM) for asymmetric transfer hydrogenation, ring-closing metathesis and anion catalysis. The additional second coordination sphere elements significantly influence both the activity and the selectivity of the resulting hybrid catalysts. These findings lead to the identification of propitious chimeric streptavidins for future directed evolution efforts of artificial metalloenzymes.

KW - anion π catalysis

KW - artificial metalloenzyme

KW - chimeric protein

KW - protein design

KW - protein engineering

KW - ring-closing metathesis

KW - transfer hydrogenation

U2 - 10.1021/acscatal.7b03773

DO - 10.1021/acscatal.7b03773

M3 - Article

AN - SCOPUS:85041420054

SN - 2155-5435

VL - 8

SP - 1476

EP - 1484

JO - ACS Catalysis

JF - ACS Catalysis

IS - 2

ER -

Chimeric streptavidins as host proteins for artificial metalloenzymes

Abstract / Description of output

Keywords / Materials (for Non-textual outputs)

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