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Differences in the dynamics of oxidized and reduced cytochrome c measured by Mössbauer spectroscopy

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Abstract

 The temperature dependence of the mean square displacement of the iron atom in reduced and oxidized cytochrome c has been studied by Mössbauer spectroscopy. The flexibility of the protein, labeled by the modes coupling to the iron, is diminished upon reduction. The differences in flexibility are sufficient to explain the differences in physicochemical properties between the oxidized and the reduced forms.

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Authors and Affiliations

  1. Institute of Chemical Physics RAS, 142432 Chernogolovka, Moskowskaja Oblast, Noginski Rajon, Russia, , , , , , RU

    E. N. Frolov & R. Gvosdev

  2. N.N. Semenov Institute of Chemical Physics RAS, 117977 Moscow, ul. Kosygina 4, Russia, , , , , , RU

    V. I. Goldanskii

  3. Fakultät für Physik E-17, Technische Universität München, D-85747 Garching, Germany Fax: +49-089-289 12548; e-mail: fgp@hexa.e17.physik.tu-muenchen.de, , , , , , DE

    F. G. Parak

Authors
  1. E. N. Frolov
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  2. R. Gvosdev
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  3. V. I. Goldanskii
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  4. F. G. Parak
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Received: 17 March 1997 / Accepted: 19 August 1997

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Frolov, E., Gvosdev, R., Goldanskii, V. et al. Differences in the dynamics of oxidized and reduced cytochrome c measured by Mössbauer spectroscopy. JBIC 2, 710–713 (1997). https://doi.org/10.1007/PL00010647

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  • DOI: https://doi.org/10.1007/PL00010647

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