Co-operative ionisation of aspartic-acid-158 and histidine-159 in papain. Evidence from 19F nuclear-magnetic-resonance and fluorescence spectroscopy

Eur J Biochem. 1976 Jun 1;65(2):481-91. doi: 10.1111/j.1432-1033.1976.tb10364.x.

Abstract

The chemical shift of the single resonance in the 19F nuclear magnetic resonance spectrum of papain which has been irreversibly inhibited by 3-bromo-1,1,1-trifluoropropanone, exhibits pH-dependence. The fluorescence intensity of this papain derivative shows pH-dependence on two groups which exhibit co-operative ionisation. This co-operative behaviour is probably a function of the probe since the fluorescence intensity of S-ethane-thio-papain is dependent on a single ionisation constant, whereas that of S-(2-hydroxyethane)-thio-papain is dependent on two ionisable groups again acting co-operatively. The 1,1,1-trifluoroketone probe will be hydrated in aqueous solution and would be capable of hydrogen bonding with the protein. The two groups detected are considered to be aspartic-acid-158 and histidine-159. The co-operative ionisation of these groups in substrate hydrolysis is discussed.

MeSH terms

  • Aspartic Acid*
  • Chemical Phenomena
  • Chemistry
  • Fluorine
  • Histidine*
  • Hydrolysis
  • In Vitro Techniques
  • Ions
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Papain*
  • Spectrometry, Fluorescence
  • Sulfhydryl Compounds / chemical synthesis

Substances

  • Ions
  • Sulfhydryl Compounds
  • Fluorine
  • Aspartic Acid
  • Histidine
  • Papain