Startseite Azobenzene switch with a long-lived cis-state to photocontrol the enzyme activity of a histone deacetylase-like amidohydrolase
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Azobenzene switch with a long-lived cis-state to photocontrol the enzyme activity of a histone deacetylase-like amidohydrolase

  • Michael Korbus , Ganesh Balasubramanian , Florian Müller-Plathe , Harald Kolmar und Franz-Josef Meyer-Almes EMAIL logo
Veröffentlicht/Copyright: 21. November 2013

Abstract

The control of enzymes by use of an external stimulus such as light enables the temporal and spatial regulation of defined chemical reactions in a highly precise manner. In this work we investigated and characterized the reversible photocontrol of a bacterial histone deacetylase-like amidohydrolase (HDAH) from Bordetella/Alcaligenes strain FB188, which holds great potential to control deacetylation reactions of a broad spectrum of substrates in biotechnological and biomedical applications. Several HDAH variants with a single surface accessible cysteine close to the active site were developed and covalently modified by a monofunctional azobenzene-based photoswitch [4-phenylazomaleinanil (4-PAM)]. The enzymatic activity of three HDAH variants (M30C, S20C and M150C) were shown to be controlled by light. The thermal cis-to-trans relaxation of azobenzene conjugated to HDAH was up to 50-fold retarded compared to unbound 4-PAM allowing light pulse switching rather than continuing irradiation to maintain the thermodynamically less stable cis-state of covalently attached 4-PAM.


Corresponding author: Franz-Josef Meyer-Almes, Department of Chemical Engineering and Biotechnology, University of Applied Sciences Darmstadt, 64287 Darmstadt, Germany, e-mail:

Acknowledgments

This work was supported by a grant of the hessian Landes-Offensive zur Entwicklung Wissenschaftlich-ökonomischer Exzellenz (LOEWE Soft Control).

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Received: 2013-8-30
Accepted: 2013-11-19
Published Online: 2013-11-21
Published in Print: 2014-4-1

©2014 by Walter de Gruyter Berlin/Boston

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