The role of the gulose-mannose part of bleomycin in activation of iron-molecular oxygen complexes

Biochem J. 1988 Jul 15;253(2):497-504. doi: 10.1042/bj2530497.

Abstract

A comparison of the complexing properties of metal ions and O2 activation by bleomycin-A2 (BLM-A2) and deglyco-BLM-A2 is presented. Deglyco-BLM-A2 is obtained from the parent derivative by HF cleavage of the sugar moiety followed by h.p.l.c. purification. Complexing of Cu(II) and Fe(III) is studied by using c.d. and e.s.r. spectroscopy. Spin-trapping experiments in the presence of phenyl N-t-butylnitrone indicated lower production of free radicals by deglyco-BLM-A2. Finally, a proposal is made to explain this discrepancy, focusing on the probable role of the gulose-mannose moiety acting as a protecting pocket, comparable with the pocket and picket-fence porphyrins described for haemoproteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bleomycin / metabolism*
  • Chromatography, High Pressure Liquid
  • Circular Dichroism
  • Copper / metabolism
  • Electron Spin Resonance Spectroscopy
  • Free Radicals
  • Hexoses
  • Iron / metabolism*
  • Macromolecular Substances
  • Mannose
  • Mass Spectrometry
  • Models, Chemical
  • Oxygen / metabolism*

Substances

  • Free Radicals
  • Hexoses
  • Macromolecular Substances
  • Bleomycin
  • gulose
  • Copper
  • Iron
  • Mannose
  • Oxygen