S
Susanne Döpner
Researcher at Max Planck Society
Publications - 14
Citations - 542
Susanne Döpner is an academic researcher from Max Planck Society. The author has contributed to research in topics: Cytochrome c & Resonance Raman spectroscopy. The author has an hindex of 9, co-authored 14 publications receiving 528 citations. Previous affiliations of Susanne Döpner include University of British Columbia.
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Journal ArticleDOI
Alkaline Conformational Transitions of Ferricytochrome c Studied by Resonance Raman Spectroscopy
TL;DR: In this article, the pH-dependent conformational equilibria of iso-1-ferricytochrome c that occur between pH 7 and pH 12 have been studied by resonance Raman (RR) spectroscopy.
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The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase.
Susanne Döpner,Peter Hildebrandt,Federico I. Rosell,A. Grant Mauk,Matthias Walter,Gerhard Buse,Tewfik Soulimane +6 more
TL;DR: The interactions of yeast iso-1 cytochrome c with bovine cy tochrome c oxidase were studied using cyto chrome c variants in which lysines of the binding domain were substituted by alanines, leading to the conclusion that the interprotein electron transfer rate constant is around two times higher in state B2 than in B1.
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FeIII‐Hydroperoxo and Peroxo Complexes with Aminopyridyl Ligands and the Resonance Raman Spectroscopic Identification of the Fe−O and O−O Stretching Modes
A. Jalila Simaan,Susanne Döpner,Frédéric Banse,Sophie Bourcier,Guy Bouchoux,Alain Boussac,Peter Hildebrandt,Jean-Jacques Girerd +7 more
TL;DR: In this paper, the spectral properties of nonheme Fe(III)-peroxo complexes with aminopyridyl-type ligands have been characterized by UV/Vis, EPR, mass and Resonance Raman spectroscopy.
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Analysis of vibrational spectra of multicomponent systems. Application to pH-dependent resonance Raman spectra of ferricytochrome c
TL;DR: In this paper, a method is presented which is appropriate to analyse complex vibrational spectra of molecular systems including several components, and the method which is related to global analysis is directed to determine the spectras of the individual components together with their relative contributions in a given set of vibration spectra.
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Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c.
TL;DR: Spectroscopic characterization of this high-spin reaction intermediate suggests that in addition to an obligatory pentacoordinate heme iron, a group within the heme pocket coordinates theHeme iron but is then replaced either by Met80, to revert to the native conformation, or by Lys73 or Lys79, to yield one of the conventional alkaline conformers.