Spectroscopic Observation of Calcium‐Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity

• DOI: 10.1002/cphc.201500112
• Publication Date: 2015-04-23T12:29:30Z
• Authors: Patrycja Kielb; Murat Sezer; Sagie Katz; Francesca Lopez; Christopher Schulz; Lo Gorton; Roland Ludwig; Ulla Wollenberger; Ingo Zebger; Inez M. Weidinger
• Keywords: Cellobiose dehydrogenase

Cellobiose dehydrogenase catalyzes the oxidation of various carbohydrates and is considered as a possible anode catalyst in biofuel cells. It has been shown that catalytic performance this enzyme immobilized on electrodes can be increased by presence calcium ions. To get insight into Ca(2+) -induced changes we employ surface-enhanced vibrational (SERR SEIRA) spectroscopy together with electrochemistry. Upon addition ions electrochemical measurements show shift turnover signal to more negative potentials while SERR reveal an offset between potential heme reduction current. Comparing SEIRA data propose binding induces protein reorientation way electron transfer pathway FAD center electrode bypass cofactor, resulting activity at potentials.