Cover image for Vol. 19 Issue 4

Editor: Greta Heydenrych; Editorial Board Chairs: Christian Amatore, Michael Grätzel, Michel Orrit

Impact Factor: 3.075

ISI Journal Citation Reports © Ranking: 2016: 8/36 (Physics Atomic Molecular & Chemical); 55/146 (Chemistry Physical)

Online ISSN: 1439-7641

Associated Title(s): Advanced Materials, ChemBioChem, ChemCatChem, ChemElectroChem, ChemPhotoChem, ChemSusChem, Small

11_13/2010Cover Picture: Cellobiose Dehydrogenase: A Versatile Catalyst for Electrochemical Applications (ChemPhysChem 13/2010)

The picture shows electron-transfer pathways between a sugar substrate (aldose) oxidized by cellobiose dehydrogenase (CDH) and an electrode. CDH is a two-domain oxidoreductase with a larger FAD-containing (FAD: flavin adenine dinucleotide, shown in yellow) dehydrogenase domain connected through a linker region to a smaller heme-b-containing (shown in red) cytochrome domain. Two electrons are initially donated by the substrate (aldose) to the catalytic domain. The electrons are then transferred to the electrode either in the direct electron transfer (DET) mode via the heme or in the mediated electron transfer (MET) mode through the help of small redox mediator molecules (light blue). On p. 2674, L. Gorton et al. review the biochemical and bioelectrochemical chacteristics of CDH as well as those biosensors and biofuel-cell anodes based on CDH and the possible use of this enzyme in bioelectrosynthesis.

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