Electrochemical activity of cytochrome P450 1A2: the relevance of O2 control and the natural electron donor

Silveira, Célia M., Rodrigues, Patrícia R., Ghach, Wissam, Pereira, Sofia A., Esteves, Francisco, Kranendonk, Michel, Etienne, Mathieu and Almeida, M. Gabriela 2021. Electrochemical activity of cytochrome P450 1A2: the relevance of O2 control and the natural electron donor. ChemElectroChem 8 (3) , pp. 500-507. 10.1002/celc.202001255

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Abstract

The direct electrochemical response of membrane-bound human cytochrome P450 1A2 (CYP1A2) was studied on pyrolytic graphite electrodes, while encapsulated in a sol-gel matrix. The enzymatic reduction of O2 was evaluated in the presence and absence of its electron donor partner, cytochrome P450 oxidoreductase (CPR). When used without CPR, CYP1A2 was shown to be highly sensitive to O2 even in the presence of residual amounts. Under aerobic conditions (air-saturated solutions), the catalytic signal attributed to the reaction with O2 was lost, suggesting the enzyme was inactivated. In contrast, the CYP1A2/CPR complex retained O2 reductase activity with high O2 concentration in solution. The results demonstrated a crucial role of CPR in stabilizing the immobilized CYP1A2 enzyme and in the preservation of O2 electrocatalysis, when using this electrochemical set-up. Though the enzyme's monooxygenase activity towards caffeine was not detected, this study highlights the complexity of coupling CYP1A2 reduction currents with substrate turnover, owing to the simultaneous electrochemical measurement of the O2 reduction reaction.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Publisher:	Wiley
ISSN:	2196-0216
Date of First Compliant Deposit:	25 August 2021
Date of Acceptance:	1 February 2021
Last Modified:	31 Aug 2021 14:00
URI:	https://orca.cardiff.ac.uk/id/eprint/143655

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