2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer

Christoph Nowak, Thamara Laredo, Jens Gebert, Jacek Lipkowski, Robert B Gennis, Shelagh Ferguson-Miller, Wolfgang Knoll, Renate L C Naumann

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)619-627
Number of pages9
JournalMetallomics
Volume3
Issue number6
DOIs
StatePublished - Jun 1 2011

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ASJC Scopus subject areas

  • Biomaterials
  • Metals and Alloys
  • Chemistry (miscellaneous)
  • Biochemistry
  • Biophysics

Cite this

Nowak, C., Laredo, T., Gebert, J., Lipkowski, J., Gennis, R. B., Ferguson-Miller, S., Knoll, W., & Naumann, R. L. C. (2011). 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer. Metallomics, 3(6), 619-627. https://doi.org/10.1039/c0mt00083c