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) |
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Pages (from-to) | 619-627 |
Number of pages | 9 |
Journal | Metallomics |
Volume | 3 |
Issue number | 6 |
DOIs | |
State | Published - Jun 2011 |
ASJC Scopus subject areas
- General Medicine