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

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

A Kénani 1, C Bailly 1, N Helbecque 1, J P Catteau 1, R Houssin 1, J L Bernier 1, J P Hénichart 1
PMCID: PMC1149325  PMID: 2460080

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.

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Selected References

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