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Electrochemical Activity of Cytochrome P450 1A2: The Relevance of O 2 Control and the Natural Electron Donor
Author(s) -
Silveira Célia M.,
Rodrigues Patrícia R.,
Ghach Wissam,
Pereira Sofia A.,
Esteves Francisco,
Kranendonk Michel,
Etienne Mathieu,
Almeida M. Gabriela
Publication year - 2021
Publication title -
chemelectrochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.182
H-Index - 59
ISSN - 2196-0216
DOI - 10.1002/celc.202001615
Subject(s) - cyp1a2 , electron transfer , cytochrome p450 , chemistry , electrochemistry , monooxygenase , biosensor , cover (algebra) , oxidoreductase , cytochrome c , enzyme , biochemistry , photochemistry , electrode , engineering , apoptosis , mechanical engineering
Abstract Invited for this month's cover picture is the Group of Biomarkers and Biosensors – GB2 ( https://gb29.webnode.pt ) at Universidade NOVA de Lisboa (Portugal) and CiiEM (Portugal). The cover picture shows the electrochemical response of the human monooxygenase enzyme, cytochrome P450 1A2 (CYP1A2), in the presence of its natural electron donor partner, cytochrome P450 oxidoreductase (CPR), highlighting the role of the interaction with the latter in the stabilization of CYP1A2 and attaining the electrochemically driven activity towards O 2 . The picture also emphasizes the protein entrapment matrix, a biocompatible sol‐gel film, which proved to be crucial for the achievement of interfacial electron transfer. Read the full text of the Article at 10.1002/celc.202001255.

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