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Eliane Nabedryk
Researcher at University of Zurich
Publications - 54
Citations - 2495
Eliane Nabedryk is an academic researcher from University of Zurich. The author has contributed to research in topics: Photosynthetic reaction centre & Rhodobacter sphaeroides. The author has an hindex of 29, co-authored 54 publications receiving 2428 citations.
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Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c.
TL;DR: Fourier-transform infrared spectroscopy has been used together with direct electrochemistry of the protein at a modified metal electrode surface and the resulting reduced-minus-oxidized infrared difference spectra show the changes in the frequencies and intensities of molecular vibrations which arise from the redox-linked conformational change.
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Binding sites of quinones in photosynthetic bacterial reaction centers investigated by light-induced FTIR difference spectroscopy: assignment of the interactions of each carbonyl of QA in Rhodobacter sphaeroides using site-specific 13C-labeled ubiquinone.
TL;DR: Light-induced QA-/QA FTIR difference spectra of the photoreduction of the primary quinone (QA) have been obtained for Rhodobacter sphaeroides reaction centers reconstituted with ubiquin one (Q3) labeled selectively with 13C at the 1- or 4-position of the quin one ring, i.e., on either of the two carbonyls.
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Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria
TL;DR: The IR spectra of the bacteriochlorophyll a and b cations and the bacteriopheophytin a andb anions were obtained by using an IR and optically transparent electrochemical cell and prominent effects of radical formation on the vibrational spectra were found.
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Characterization by FTIR spectroscopy of the photoreduction of the primary quinone acceptor QA in photosystem II
TL;DR: Molecular changes associated with the photoreduction of the primary quinone acceptor Qa of photosystem II have been characterized by Fourier transform infrared spectroscopy and stabilization of QA − does not result from a large protein conformation change, but involves perturbations of several amino acid vibrations.
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A new infrared electronic transition of the oxidized primary electron donor in bacterial reaction centers: a way to assess resonance interactions between the bacteriochlorophylls.
TL;DR: A broad absorption band with the predicted properties was found in a previously unexplored region of the spectrum, found in reaction centers of Rhodobacter sphaeroides and several other species of bacteria that contain bacteriochlorophyll a, and near 2750 cm-1 in Rhodopseudomonas viridis.