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Advances in High Pressure Bioscience and Biotechnology pp 203–206Cite as

The Dynamics of Protein-Bound Water in the Heme Domain of P450BM3 as Compared with P450cam and P450 2B4

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Abstract

Pressure-induced transitions in the heme domain of cytochrome P450 BM3 (P450BMP) and P450cam were studied versus the concentration of their substrates (palmitic acid and camphor). The barotropic behavior of these bacterial proteins are compared with that of rabbit liver microsomal P450 2B4. General regularities and differencies in the dynamics of proteinbound water in these hemoproteins are discussed.

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References

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Author information

Authors and Affiliations

  1. Institute of Biomedical Chemistry, 10 Pogodinskaya, 119832, Moscow, Russia

    D. R. Davydov

  2. Institut de Biologie Physico-Chimique, INSERM Unité 310, Paris, France

    G. Hui Bon Hoa

  3. Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX, USA

    J. A. Peterson

Authors
  1. D. R. Davydov
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  2. G. Hui Bon Hoa
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  3. J. A. Peterson
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Editor information

Editors and Affiliations

  1. Section Physical Chemistry, University of Heidelberg, Institute for Pharmaceutical Technology and Biopharmacy, Im Neuenheimer Feld 346, D -69120, Heidelberg, Germany

    Horst Ludwig

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© 1999 Springer-Verlag Berlin Heidelberg

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Cite this paper

Davydov, D.R., Hui Bon Hoa, G., Peterson, J.A. (1999). The Dynamics of Protein-Bound Water in the Heme Domain of P450BM3 as Compared with P450cam and P450 2B4. In: Ludwig, H. (eds) Advances in High Pressure Bioscience and Biotechnology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60196-5_44

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  • DOI: https://doi.org/10.1007/978-3-642-60196-5_44

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-64300-2

  • Online ISBN: 978-3-642-60196-5

  • eBook Packages: Springer Book Archive

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