Abstract
Induced chirality (achiral target in chiral matrix such as proteins) sometimes play a useful role in evaluating supramolecular systems involving biomolecules. Enzymatic fuel cells, which generate electricity via enzymatic redox reactions at electrodes hold a significant potential for sustainable power. Bacterial laccase, a multi-copper oxidase, was used in the cathodic compartment of the enzymatic biofuel cells because of its low redox potential. Three new salen Cu(II) complexes were designed and investigated as mediators. The Schiff base ligands consisted of both a redox-active (anthraquinone) and a photochromic (azobenzene) moiety. The interaction between laccase and a mediator was examined with induced circular dichroism (CD) and the docking tool to observe in which of the laccase domains the mediators bind as well as study the photo-induced tuning of both the cis-trans photoisomerization and orientation by the Weigert effect. Both the electrochemical and photochromic properties are also discussed and compared using density functional theory (DFT), time-dependent (TD)-DFT, and docking simulations.
Highlights
Laccase is an enzyme that catalyzes the four-electron reduction of oxygen to water through four copper atoms
Multicopper oxidase such as laccase is used as an enzyme on the cathode side of the enzyme-type biofuel cell [4,5,6,7]
The present study suggested an experimental fact of salen-type mediator’s molecular orientation dependence of electron transfer for the first time
Summary
Laccase is an enzyme that catalyzes the four-electron reduction of oxygen to water through four copper atoms. A protein that includes copper atoms is referred to as multicopper oxidase [1,2,3]. The four copper atoms that are the active sites of the laccase are divided into three types (T1–T3) and. T1 copper first receives electrons from the substrate and oxidizes the substrate, which is followed by a four-electron reduction at the T2 and. Multicopper oxidase such as laccase is used as an enzyme on the cathode side of the enzyme-type biofuel cell [4,5,6,7]. There is a drawback that enzyme stability is lacking, and the electric power is smaller than that of other fuel cells. A mediator that assists the donation and reception of the electron has been used for electron transfer between the Symmetry 2020, 12, 797; doi:10.3390/sym12050797 www.mdpi.com/journal/symmetry
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
