Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides

Andreas Schwaighofer; Christoph Steininger; M. David Hildenbrandt; Johannes Srajer; Christoph Nowak; Wolfgang Knoll; Renate L. C. Naumann

doi:10.1016/j.bpj.2013.10.037

Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides

Andreas Schwaighofer
, Christoph Steininger
, M. David Hildenbrandt
, Johannes Srajer
, Christoph Nowak
, Wolfgang Knoll
, Renate L. C. Naumann

Publikation: Beitrag in Fachzeitschrift › Artikel › Begutachtung

Abstract

Time-resolved surface-enhanced IR-absorption spectroscopy triggered by electrochemical modulation has been performed on cytochrome c oxidase from Rhodobacter sphaeroides. Single bands isolated from a broad band in the amide I region using phase-sensitive detection were attributed to different redox centers. Their absorbances changing on the millisecond timescale could be fitted to a model based on protonation-dependent chemical reaction kinetics established previously. Substantial conformational changes of secondary structures coupled to redox transitions were revealed.

Originalsprache	Englisch
Seiten (von - bis)	2706-2713
Seitenumfang	8
Fachzeitschrift	Biophysical Journal
Volume	105
DOIs	https://doi.org/10.1016/j.bpj.2013.10.037
Publikationsstatus	Veröffentlicht - 2013

Research Field

Biosensor Technologies

Zugriff auf Dokument

10.1016/j.bpj.2013.10.037Lizenz: Nicht angegeben

Diese Publikation zitieren

@article{1478eee7b6144d3f9e9275fafdfeb648,

title = "Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides",

abstract = "Time-resolved surface-enhanced IR-absorption spectroscopy triggered by electrochemical modulation has been performed on cytochrome c oxidase from Rhodobacter sphaeroides. Single bands isolated from a broad band in the amide I region using phase-sensitive detection were attributed to different redox centers. Their absorbances changing on the millisecond timescale could be fitted to a model based on protonation-dependent chemical reaction kinetics established previously. Substantial conformational changes of secondary structures coupled to redox transitions were revealed.",

author = "Andreas Schwaighofer and Christoph Steininger and Hildenbrandt, \{M. David\} and Johannes Srajer and Christoph Nowak and Wolfgang Knoll and Naumann, \{Renate L. C.\}",

year = "2013",

doi = "10.1016/j.bpj.2013.10.037",

language = "English",

volume = "105",

pages = "2706--2713",

journal = "Biophysical Journal",

issn = "0006-3495",

publisher = "Elsevier Inc.",

}

TY - JOUR

T1 - Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides

AU - Schwaighofer, Andreas

AU - Steininger, Christoph

AU - Hildenbrandt, M. David

AU - Srajer, Johannes

AU - Nowak, Christoph

AU - Knoll, Wolfgang

AU - Naumann, Renate L. C.

PY - 2013

Y1 - 2013

N2 - Time-resolved surface-enhanced IR-absorption spectroscopy triggered by electrochemical modulation has been performed on cytochrome c oxidase from Rhodobacter sphaeroides. Single bands isolated from a broad band in the amide I region using phase-sensitive detection were attributed to different redox centers. Their absorbances changing on the millisecond timescale could be fitted to a model based on protonation-dependent chemical reaction kinetics established previously. Substantial conformational changes of secondary structures coupled to redox transitions were revealed.

AB - Time-resolved surface-enhanced IR-absorption spectroscopy triggered by electrochemical modulation has been performed on cytochrome c oxidase from Rhodobacter sphaeroides. Single bands isolated from a broad band in the amide I region using phase-sensitive detection were attributed to different redox centers. Their absorbances changing on the millisecond timescale could be fitted to a model based on protonation-dependent chemical reaction kinetics established previously. Substantial conformational changes of secondary structures coupled to redox transitions were revealed.

U2 - 10.1016/j.bpj.2013.10.037

DO - 10.1016/j.bpj.2013.10.037

M3 - Article

SN - 0006-3495

VL - 105

SP - 2706

EP - 2713

JO - Biophysical Journal

JF - Biophysical Journal

ER -

Time-Resolved Surface-Enhanced IR-Absorption Spectroscopy of Direct Electron Transfer to Cytochrome c Oxidase from R. sphaeroides

Abstract

Research Field

Zugriff auf Dokument

Fingerprint

Diese Publikation zitieren