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High Pressure as Tool to Study Structural Properties of Thiolate Heme Proteins

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Advances in High Pressure Bioscience and Biotechnology II

Abstract

A membrane driven high-pressure cell with sapphire anvils is used to measure the CO ligand stretch mode of various substrate complexes of cytochrome P450cam. In situ pressure measurement is performed using the ruby R1 luminescence band using a Raman spectrometer coupled via fiber optics to the sample compartment of the FT infrared spectrometer. It was found for all substrate complexes that the CO stretch mode shifts to lower frequencies with increasing pressure. The slope of the shift is interpretated as compressibility and correlates with the high-spin state content produced by the substrates in the oxidized form of the enzyme.

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References

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Author information

Authors and Affiliations

  1. Protein Dynamics Laboratory, Max-Delbrück-Center for Molecular Medicine, D-13125, Berlin, Germany

    C. Jung

  2. Laboratoire de Physique des Milieux Condensés, Université Pierre et Marie Curie, F-75252, Paris, France

    B. Canny & J. C. Chervin

Authors
  1. C. Jung
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  2. B. Canny
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  3. J. C. Chervin
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Editor information

Editors and Affiliations

  1. Department of Chemistry, Physical Chemistry I, University of Dortmund, Otto-Hahn-Str. 6, 44227, Dortmund, Germany

    Roland Winter

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© 2003 Springer-Verlag Berlin Heidelberg

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Jung, C., Canny, B., Chervin, J.C. (2003). High Pressure as Tool to Study Structural Properties of Thiolate Heme Proteins. In: Winter, R. (eds) Advances in High Pressure Bioscience and Biotechnology II. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-05613-4_4

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  • DOI: https://doi.org/10.1007/978-3-662-05613-4_4

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-05674-1

  • Online ISBN: 978-3-662-05613-4

  • eBook Packages: Springer Book Archive

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