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Conformational equilibria and dynamics of cytochrome c induced by binding of sodium dodecyl sulfate monomers and micelles

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Abstract

Circular dichroism, nuclear magnetic resonance, electron paramagnetic resonance, UV-vis absorption, and resonance Raman (RR) spectroscopic techniques were employed to study protein and heme structural changes of cytochrome c (Cyt-c) induced by sodium dodecyl sulfate (SDS) monomers and micelles via hydrophobic and electrostatic interactions, respectively. Both modes of interactions cause the transition to the conformational state B2, which is implicated to be involved in the physiological processes of Cyt-c. At sub-micellar concentrations of SDS, specific binding of only ca. three SDS monomers, which is likely to occur at the hydrophobic peptide segment 81–85, is sufficient for a complete conversion to a B2 state in which Met80 is replaced by His33 (His26). These heme pocket structural changes are not linked to secondary structure changes of the protein brought about by nonspecific binding of SDS monomers in different regions of the protein. Upon binding of micelles, B2 high-spin species can also be stabilized by electrostatic interactions. In addition, the micelle interaction domain is located on the front surface of Cyt-c, which includes a ring-like arrangement of lysine residues appropriate for binding one micelle. According to freeze-quench RR and stopped-flow experiments, state B2 is formed on the long millisecond timescale and reveals a complex dependence on the SDS concentration that can be interpreted in terms of competitive binding of monomers and micelles.

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Acknowledgements

The authors thank Dr. E. Bill, Prof. N. Metzler-Nolte, and Dr. R. Schumacher for kind support in EPR, NMR, and stopped-flow experiments, respectively. Technical assistance by B. Deckers is gratefully acknowledged. The work was supported by the Volkswagen-Stiftung (I 72826).

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Author notes

  1. Silke Oellerich

    Present address: Huygens Laboratory, Department of Biophysics, Leiden University, Niels Bohrweg 2, 2333 CA , Leiden, The Netherlands

  2. Hainer Wackerbarth

    Present address: Biouorganisk Kemi, Danmarks Tekniske Universitet, Bygning 207, 2800 , Lyngby, Denmark

  3. Peter Hildebrandt

    Present address: Max-Volmer-Laboratorium, Institut für Chemie, Technische Universität Berlin, Sekr. PC 14, Strasse des 17 Juni 135, 10623 , Berlin, Germany

Authors and Affiliations

  1. Max-Planck-Institut für Strahlenchemie, Stiftstrasse 34–36, 45470 , Mulheim, Germany

    Silke Oellerich, Hainer Wackerbarth & Peter Hildebrandt

  2. Instituto de Tecnologica Química e Biológica, Apartado 127, Av. da República, 2781-901 , Oeiras, Portugal

    Peter Hildebrandt

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  1. Silke Oellerich
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Correspondence to Peter Hildebrandt.

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Oellerich, S., Wackerbarth, H. & Hildebrandt, P. Conformational equilibria and dynamics of cytochrome c induced by binding of sodium dodecyl sulfate monomers and micelles. Eur Biophys J 32, 599–613 (2003). https://doi.org/10.1007/s00249-003-0306-y

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