Effects of Freezing on the Coordination State and Ligand Orientation in Hemoproteins

  • Helen Anni
  • Takashi Yonetani

Abstract

Some spectroscopic and kinetic measurements of hemoproteins have been carried out in cryogenic temperatures in order to achieve a number of specific objectives such as trapping transient intermediates, retarding decay processes and electron/nuclear relaxation rates, controlling reaction rates, expanding a range of temperature, increasing signal-to-noise ratios of spectroscopic data, etc. It is generally assumed in these measurements that freezing would not adversely alter the sites and properties of interest. The absence of obvious changes in the frozen sample after thawing is sometimes taken as a proof that freezing has not irreversibly modified the protein. However, this does not exclude the possibility that a hemoprotein may be reversibly altered in frozen states due to the physical stress exerted by crystallized solvent water molecules. In addition, it is well known that pH and other physical properties of aqueous solutions could be significantly changed upon freezing1.

Keywords

Crystallization Glycerol Microwave Helium Propylene 

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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Helen Anni
    • 1
  • Takashi Yonetani
    • 1
  1. 1.Department of Biochemistry and BiophysicsUniversity of PennsylvaniaPhiladelphiaUSA

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