Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure

Sarah M. Pratter; Cornelia Konstantinovics; Cristiana M L Di Giuro; Erich Leitner; Devesh Kumar; Sam P. De Visser; Gideon Grogan; Grit D. Straganz

doi:10.1002/anie.201304633

Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure

Sarah M. Pratter, Cornelia Konstantinovics, Cristiana M L Di Giuro, Erich Leitner, Devesh Kumar, Sam P. De Visser, Gideon Grogan, Grit D. Straganz

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

Abstract

The ol' switcheroo: The enantioselectivity of an O2-dependent hydroxylation at a mononuclear non-heme iron center was switched from S to R by changing the geometry of the substrate ligand at the metal center through protein redesign. This rational approach resulted in a greater than 9000-fold enhancement in (R)-selectivity and yielded a highly active (R)-mandelate synthase. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Original language	English
Pages (from-to)	9677-9681
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	37
DOIs	https://doi.org/10.1002/anie.201304633
Publication status	Published - 9 Sept 2013

Keywords

asymmetric catalysis
hydroxylation
metalloenzymes
non-heme iron
protein design

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Pratter, S. M., Konstantinovics, C., Di Giuro, C. M. L., Leitner, E., Kumar, D., De Visser, S. P., Grogan, G., & Straganz, G. D. (2013). Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure. Angewandte Chemie - International Edition, 52(37), 9677-9681. https://doi.org/10.1002/anie.201304633

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title = "Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure",

abstract = "The ol' switcheroo: The enantioselectivity of an O2-dependent hydroxylation at a mononuclear non-heme iron center was switched from S to R by changing the geometry of the substrate ligand at the metal center through protein redesign. This rational approach resulted in a greater than 9000-fold enhancement in (R)-selectivity and yielded a highly active (R)-mandelate synthase. Copyright {\textcopyright} 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

keywords = "asymmetric catalysis, hydroxylation, metalloenzymes, non-heme iron, protein design",

author = "Pratter, {Sarah M.} and Cornelia Konstantinovics and {Di Giuro}, {Cristiana M L} and Erich Leitner and Devesh Kumar and {De Visser}, {Sam P.} and Gideon Grogan and Straganz, {Grit D.}",

note = "cited By 7",

year = "2013",

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day = "9",

doi = "10.1002/anie.201304633",

language = "English",

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Pratter, SM, Konstantinovics, C, Di Giuro, CML, Leitner, E, Kumar, D, De Visser, SP, Grogan, G & Straganz, GD 2013, 'Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure', Angewandte Chemie - International Edition, vol. 52, no. 37, pp. 9677-9681. https://doi.org/10.1002/anie.201304633

Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure. / Pratter, Sarah M.; Konstantinovics, Cornelia; Di Giuro, Cristiana M L et al.
In: Angewandte Chemie - International Edition, Vol. 52, No. 37, 09.09.2013, p. 9677-9681.

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

TY - JOUR

T1 - Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure

AU - Pratter, Sarah M.

AU - Konstantinovics, Cornelia

AU - Di Giuro, Cristiana M L

AU - Leitner, Erich

AU - Kumar, Devesh

AU - De Visser, Sam P.

AU - Grogan, Gideon

AU - Straganz, Grit D.

N1 - cited By 7

PY - 2013/9/9

Y1 - 2013/9/9

N2 - The ol' switcheroo: The enantioselectivity of an O2-dependent hydroxylation at a mononuclear non-heme iron center was switched from S to R by changing the geometry of the substrate ligand at the metal center through protein redesign. This rational approach resulted in a greater than 9000-fold enhancement in (R)-selectivity and yielded a highly active (R)-mandelate synthase. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

AB - The ol' switcheroo: The enantioselectivity of an O2-dependent hydroxylation at a mononuclear non-heme iron center was switched from S to R by changing the geometry of the substrate ligand at the metal center through protein redesign. This rational approach resulted in a greater than 9000-fold enhancement in (R)-selectivity and yielded a highly active (R)-mandelate synthase. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

KW - asymmetric catalysis

KW - hydroxylation

KW - metalloenzymes

KW - non-heme iron

KW - protein design

U2 - 10.1002/anie.201304633

DO - 10.1002/anie.201304633

M3 - Article

SN - 1433-7851

VL - 52

SP - 9677

EP - 9681

JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

IS - 37

ER -

Inversion of enantioselectivity of a mononuclear non-heme iron(II)-dependent hydroxylase by tuning the interplay of metal-center geometry and protein structure

Abstract

Keywords

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