Abstract
Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a biomimetic membrane system were followed by two-dimensional surface-enhanced IR absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was employed to vary the redox state of the enzyme. The CcO was shown to undergo a conformational transition from a non-activated to an activated state after it was allowed to turnover in the presence of oxygen. Differences between the non-activated and activated state were revealed by 2D SEIRA spectra recorded as a function of potential. The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 619-627 |
| Number of pages | 9 |
| Journal | Metallomics |
| Volume | 3 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jun 1 2011 |
Fingerprint
ASJC Scopus subject areas
- Biomaterials
- Metals and Alloys
- Chemistry (miscellaneous)
- Biochemistry
- Biophysics
Cite this
2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer. / Nowak, Christoph; Laredo, Thamara; Gebert, Jens; Lipkowski, Jacek; Gennis, Robert B; Ferguson-Miller, Shelagh; Knoll, Wolfgang; Naumann, Renate L C.
In: Metallomics, Vol. 3, No. 6, 01.06.2011, p. 619-627.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer
AU - Nowak, Christoph
AU - Laredo, Thamara
AU - Gebert, Jens
AU - Lipkowski, Jacek
AU - Gennis, Robert B
AU - Ferguson-Miller, Shelagh
AU - Knoll, Wolfgang
AU - Naumann, Renate L C
PY - 2011/6/1
Y1 - 2011/6/1
N2 - Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a biomimetic membrane system were followed by two-dimensional surface-enhanced IR absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was employed to vary the redox state of the enzyme. The CcO was shown to undergo a conformational transition from a non-activated to an activated state after it was allowed to turnover in the presence of oxygen. Differences between the non-activated and activated state were revealed by 2D SEIRA spectra recorded as a function of potential. The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer.
AB - Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a biomimetic membrane system were followed by two-dimensional surface-enhanced IR absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was employed to vary the redox state of the enzyme. The CcO was shown to undergo a conformational transition from a non-activated to an activated state after it was allowed to turnover in the presence of oxygen. Differences between the non-activated and activated state were revealed by 2D SEIRA spectra recorded as a function of potential. The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer.
UR - http://www.scopus.com/inward/record.url?scp=79959195027&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79959195027&partnerID=8YFLogxK
U2 - 10.1039/c0mt00083c
DO - 10.1039/c0mt00083c
M3 - Article
C2 - 21541411
AN - SCOPUS:79959195027
VL - 3
SP - 619
EP - 627
JO - Metallomics
JF - Metallomics
SN - 1756-5901
IS - 6
ER -