Cover Picture: Engineering of Cellobiose Dehydrogenases for Improved Glucose Sensitivity and Reduced Maltose Affinity (ChemElectroChem 4/2017). Issue 4 (16th March 2017)

• Record Type: Journal Article
• Authors: Ortiz, Roberto; Rahman, Mahbubur; Zangrilli, Beatrice; Sygmund, Christoph; Micheelsen, Pernille O.; Silow, Maria; Toscano, Miguel D.; Ludwig, Roland; Gorton, Lo
• Is Part Of: ChemElectroChem. Volume 4:Issue 4(2017)
• Page Start: 748
• Page End: 748
• Publication Date: 2017-03-16
• Subjects: cellobiose dehydrogenase -- enzymatic fuel cells -- direct electron transfer -- glucose sensors -- site-directed mutagenesis; Electrochemistry -- Periodicals; 541.37
• DOI: 10.1002/celc.201700227
• Languages: English
• ISSNs: 2196-0216

Abstract

Abstract : The Front Cover picture shows mutated cellobiose dehydrogenase (CDH) immobilized on a graphite electrode and how preferentially glucose is oxidized by this enzyme. The enzyme consists of a larger catalytic dehydrogenase domain (grey) containing FAD as cofactor (orange) and a smaller cytochrome domain (lavender) containing heme as cofactor (yellow) connected through a linker region (green). The two electrons transferred from glucose to FAD in the catalytic reaction are then sequentially transferred from FAD to heme and, from there, directly to the electrode in a mediatorless fashion. The CDH in the picture is a mutant specially made to drastically decrease the affinity of the enzyme for maltose to minimize false readout values of blood of diabetic patients. More information can be found in the Article by R. Ortiz, L. Gorton, and co‐workers onpage 846 in Issue 4, 2017 (DOI:10.1002/celc.201600781 ).