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

Kielb, Patrycja; Sezer, Murat; Katz, Sagie; Lopez, Francesca; Schulz, Christopher LU ; Gorton, Lo LU ; Ludwig, Roland; Wollenberger, Ulla; Zebger, Ingo and Weidinger, Inez M. (2015) In ChemPhysChem 16(9). p.1960-1968
Abstract
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
cellobiose dehydrogenase, electron transfer, enzyme catalysis, spectroelectrochemistry, surface-enhanced vibrational spectroscopy
in
ChemPhysChem
volume
16
issue
9
pages
1960 - 1968
publisher
John Wiley & Sons
external identifiers
  • wos:000356714800023
  • scopus:84934922774
ISSN
1439-7641
DOI
10.1002/cphc.201500112
language
English
LU publication?
yes
id
73322d59-0908-463e-8b16-b00bd7a9ea26 (old id 7596824)
date added to LUP
2015-07-23 11:30:32
date last changed
2017-09-24 03:07:45
@article{73322d59-0908-463e-8b16-b00bd7a9ea26,
  abstract     = {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.},
  author       = {Kielb, Patrycja and Sezer, Murat and Katz, Sagie and Lopez, Francesca and Schulz, Christopher and Gorton, Lo and Ludwig, Roland and Wollenberger, Ulla and Zebger, Ingo and Weidinger, Inez M.},
  issn         = {1439-7641},
  keyword      = {cellobiose dehydrogenase,electron transfer,enzyme catalysis,spectroelectrochemistry,surface-enhanced vibrational spectroscopy},
  language     = {eng},
  number       = {9},
  pages        = {1960--1968},
  publisher    = {John Wiley & Sons},
  series       = {ChemPhysChem},
  title        = {Spectroscopic Observation of Calcium-Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity},
  url          = {http://dx.doi.org/10.1002/cphc.201500112},
  volume       = {16},
  year         = {2015},
}