Autori: Vasile Coman, Wolfgang Harreither, Roland Ludwig, Dietmar Haltrich, Lo Gorton

Editorial: Chemia Analityczna (Warsaw), 52, p.945-960, 2007.

Rezumat:

Cellobiose dehydrogenase (CDH) is a monomeric protein consisting of two subdomains: a larger flavin-associated domain (DHcdh) and a smaller heme-binding domain (CYTcdh), connected via a protease cleavable linker region. In this study, the inter-domain electron transfer, using the CDH from the ascomycete fungus Myriococcum thermophilum and thiol (SAM) modified gold electrodes, was investigated with cyclic voltammetry and UV-Vis spectroelectrochemistry. The effect of the SAM and pH on the formal potential of the heme domain of CDH and on the current generated by the electrocatalytic oxidation of cellobiose and lactose was evaluated with voltammetric techniques. The oxidation-reduction midpoint potentials of the DHcdh, CYTcdh, and whole CDH unit were estimated at different pH values using a long-optical-pathway thin capillary-type spectroelectrochemical cell.

Cuvinte cheie: Cellobiose Dehydrogenase, Myriococcum thermophilum, Thiol Modified Gold Electrode, Direct Electron Transfer, Bioelectrocatalysis