Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides

Andreas Schwaighofer; Christoph Steininger; David M 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

Biophys J. 2013 Dec 17;105(12):2706-13. doi: 10.1016/j.bpj.2013.10.037.

Authors

Andreas Schwaighofer¹, Christoph Steininger¹, David M Hildenbrandt¹, Johannes Srajer², Christoph Nowak², Wolfgang Knoll¹, Renate L C Naumann³

Affiliations

¹ Austrian Institute of Technology, Vienna, Austria.
² Austrian Institute of Technology, Vienna, Austria; Center of Electrochemical Surface Technology, Wiener Neustadt, Austria.
³ Austrian Institute of Technology, Vienna, Austria. Electronic address: Renate.Naumann@ait.ac.at.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry
Bacterial Proteins / metabolism*
Electron Transport
Electron Transport Complex IV / chemistry
Electron Transport Complex IV / metabolism*
Electrons*
Rhodobacter sphaeroides / enzymology*
Rhodobacter sphaeroides / metabolism
Spectroscopy, Fourier Transform Infrared

Substances

Bacterial Proteins
Electron Transport Complex IV