TY  - JOUR
A1  - Kielb, Patrycja
A1  - Sezer, Murat
A1  - Katz, Sagie
A1  - Lopez, Francesca
A1  - Schulz, Christopher
A1  - Gorton, Lo
A1  - Ludwig, Roland
A1  - Wollenberger, Ursula
A1  - Zebger, Ingo
A1  - Weidinger, Inez M.
T1  - Spectroscopic Observation of Calcium-Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity
JF  - ChemPhysChem : a European journal of chemical physics and physical chemistry
N2  - Cellobiose dehydrogenase catalyzes the oxidation of various carbohydrates and is considered as a possible anode catalyst in biofuel cells. It has been shown that the catalytic performance of this enzyme immobilized on electrodes can be increased by presence of calcium ions. To get insight into the Ca2+-induced changes in the immobilized enzyme we employ surface-enhanced vibrational (SERR and SEIRA) spectroscopy together with electrochemistry. Upon addition of Ca2+ ions electrochemical measurements show a shift of the catalytic turnover signal to more negative potentials while SERR measurements reveal an offset between the potential of heme reduction and catalytic current. Comparing SERR and SEIRA data we propose that binding of Ca2+ to the heme induces protein reorientation in a way that the electron transfer pathway of the catalytic FAD center to the electrode can bypass the heme cofactor, resulting in catalytic activity at more negative potentials.
KW  - cellobiose dehydrogenase
KW  - electron transfer
KW  - enzyme catalysis
KW  - spectroelectrochemistry
KW  - surface-enhanced vibrational spectroscopy
Y1  - 2015
U6  - https://doi.org/10.1002/cphc.201500112
SN  - 1439-4235
SN  - 1439-7641
VL  - 16
IS  - 9
SP  - 1960
EP  - 1968
PB  - Wiley-VCH
CY  - Weinheim
ER  -