In situ modulation of enzyme activity via heterogeneous catalysis utilizing solid electroplated cofactors

[Display omitted] •Mechanistic aspects of the electroplating of cofactors from multiple electrolytes were studied.•The role of polymer binding agents on cofactors attachment was revealed.•The architecture of the hybrid electrodes was realized by methods of quantum chemistry.•The immobilized cofactor...

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Published inComputational and structural biotechnology journal Vol. 20; pp. 3824 - 3832
Main Authors Apushkinskaya, N., Zolotukhina, E.V., Butyrskaya, E.V., Silina, Y.E.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.01.2022
Research Network of Computational and Structural Biotechnology
Elsevier
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Summary:[Display omitted] •Mechanistic aspects of the electroplating of cofactors from multiple electrolytes were studied.•The role of polymer binding agents on cofactors attachment was revealed.•The architecture of the hybrid electrodes was realized by methods of quantum chemistry.•The immobilized cofactors remain biologically active and can be used for reconstituting of the enzyme structure. During product isolation the received bioreceptors often do not exhibit a sufficient biochemical activity due to multistep dissociation and loss of cofactors. However, for bioelectrochemical applications the presence of cofactors is necessary for a successful oxidative or reductive conversion of the substrates to the products. Herein, we show how the immobilization of the required electroplated cofactors in a design of amperometric electrodes can in situ assist the activity of apo-enzymes. Compared to conventional approaches used in enzyme engineering this tailored nanoengineering methodology is superior from economic point of view, labor and time costs, storage conditions, reduced amount of waste and can fill the gap in the development of tuned bioelectrocatalysts.
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ISSN:2001-0370
2001-0370
DOI:10.1016/j.csbj.2022.07.012