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Biophysical Journal 63: 1605-1612 (1992)
© 1992 the Biophysical Society

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Softening of the packing density of horseradish peroxidase by a H-donor bound near the heme pocket

J. Fidy *, J. M. Vanderkooi {ddagger}, J. Zollfrank § and J. Friedrich §

Institute of Biophysics, Semmelweis Medical University, Budapest, H-1444, Hungary
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Physikalisches Institut und Bayreuther Institut für Makromolekülforschung, Universität Bayreuth, D-8580 Bayreuth, Germany

ABSTRACT

We use pressure tuning of spectral holes to estimate the compressibility of protein molecules by optical means. We found that the compressibility of mesoporphyrin-substituted horseradish peroxidase increases by a factor of three when it incorporates small aromatic H-donor molecules that bind in the vicinity of its heme pocket. Such a dramatic softening of its packing density corresponds to a jump from a compressibility range characteristic for the solid state into that characteristic for liquids.




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I. Renge, R. van Grondelle, and J. P. Dekker
Pigment Spectra and Intermolecular Interaction Potentials in Glasses and Proteins
Biophys. J., October 1, 2007; 93(7): 2491 - 2503.
[Abstract] [Full Text] [PDF]




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Copyright © 1992 by the Biophysical Society.