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

doi:10.1039/c0mt00083c

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

Biochemistry

Research output: Contribution to journal › Article › peer-review

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	https://doi.org/10.1039/c0mt00083c
State	Published - Jun 2011

ASJC Scopus subject areas

Chemistry (miscellaneous)
Biophysics
Biomaterials
Biochemistry
Metals and Alloys

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10.1039/c0mt00083c

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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.",

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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

Y1 - 2011/6

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.

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

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