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Surface characterization and direct electrochemistry of redox copper centers of bilirubin oxidase from fungi Myrothecium verrucaria by Dmitri Ivnitski; Kateryna Artyushkova; Plamen Atanassov is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Redox potentials of T1 and T2/T3 copper centers Direct electron transfer Angle-resolved XPS The key characteristics of multicopper oxidases are redox potentials of Type 1, Type 2 and Type 3 copper centers of enzymes. However, there is still a challenge to obtain a value of the redox "signature" of the enzymes. In this study, the electrochemical behavior of T1 and T2/T3 redox copper centers of bilirubin oxidase (BOD) from the fungi Myrothecium verrucaria was studied based on direct bioelectrocatalysis. Two distinct redox peaks corresponding to reduction and oxidation of T1 and T2/T3 redox centers of enzymes have been clearly detected in anaerobic conditions. The bioelectrocatalytic activity of the enzyme was studied in the presence of oxygen and redox mediators. The electron-transfer rate constant for BOD immobilized on carbon electrode (CE) is 1.5 s -1 . The mechanism of enzyme inactivation by ABTS has been proposed. The physical architecture of BOD layers immobilized on the electrode surface, including elemental and chemical composition, relative thickness and assembly of layers was investigated by Angle Resolved Xray photoelectron spectroscopy. Unique peaks of BOD at 288.5 eV and

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Author

Dmitri Ivnitski; Kateryna Artyushkova; Plamen Atanassov

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1567-5394)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Physical Sciences)