How Mg2+ ions lower the SN2@P barrier in enzymatic triphosphate hydrolysis

Marc A. Van Bochove; Goedele Roos; Célia Fonseca Guerra; Trevor A. Hamlin; F. Matthias Bickelhaupt

doi:10.1039/c8cc00700d

How Mg²⁺ ions lower the S_N2@P barrier in enzymatic triphosphate hydrolysis

Marc A. Van Bochove, Goedele Roos, Célia Fonseca Guerra, Trevor A. Hamlin, F. Matthias Bickelhaupt

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

18 Citations (Scopus)

Abstract

Our quantum chemical activation strain analyses demonstrate how Mg²⁺ lowers the barrier of the enzymatic triphosphate hydrolysis through two distinct mechanisms: (a) weakening of the leaving-group bond, thereby decreasing activation strain; and (b) transition state (TS) stabilization through enhanced electrophilicity of the triphosphate PPP substrate, thereby strengthening the interaction with the nucleophile.

Original language	English
Pages (from-to)	3448-3451
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	28
DOIs	https://doi.org/10.1039/c8cc00700d
Publication status	Published - 11 Apr 2018
Externally published	Yes

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/c8cc00700d

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abstract = "Our quantum chemical activation strain analyses demonstrate how Mg2+ lowers the barrier of the enzymatic triphosphate hydrolysis through two distinct mechanisms: (a) weakening of the leaving-group bond, thereby decreasing activation strain; and (b) transition state (TS) stabilization through enhanced electrophilicity of the triphosphate PPP substrate, thereby strengthening the interaction with the nucleophile.",

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AU - Van Bochove, Marc A.

AU - Roos, Goedele

AU - Fonseca Guerra, Célia

AU - Hamlin, Trevor A.

AU - Bickelhaupt, F. Matthias

PY - 2018/4/11

Y1 - 2018/4/11

N2 - Our quantum chemical activation strain analyses demonstrate how Mg2+ lowers the barrier of the enzymatic triphosphate hydrolysis through two distinct mechanisms: (a) weakening of the leaving-group bond, thereby decreasing activation strain; and (b) transition state (TS) stabilization through enhanced electrophilicity of the triphosphate PPP substrate, thereby strengthening the interaction with the nucleophile.

AB - Our quantum chemical activation strain analyses demonstrate how Mg2+ lowers the barrier of the enzymatic triphosphate hydrolysis through two distinct mechanisms: (a) weakening of the leaving-group bond, thereby decreasing activation strain; and (b) transition state (TS) stabilization through enhanced electrophilicity of the triphosphate PPP substrate, thereby strengthening the interaction with the nucleophile.

UR - https://www.scopus.com/pages/publications/85044858636

U2 - 10.1039/c8cc00700d

DO - 10.1039/c8cc00700d

M3 - Article

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AN - SCOPUS:85044858636

SN - 1359-7345

VL - 54

SP - 3448

EP - 3451

JO - Chemical Communications

JF - Chemical Communications

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ER -

How Mg²⁺ ions lower the S_N2@P barrier in enzymatic triphosphate hydrolysis

Abstract

ASJC Scopus subject areas

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