Inhibition of protohaem ferro-lyase by N-substituted porphyrins. Structural requirements for the inhibitory effect

Biochem J. 1980 Sep 1;189(3):645-8. doi: 10.1042/bj1890645.

Abstract

N-Methyl mesoporphyrin was a powerful inhibitor of protohaem ferro-lyase in vitro, whereas N-ethyl mesoporphyrin and N-methyl coproporphyrin were not and neither was the newly described green pigment produced by giving rats ethylene. This suggests that the size of the substituent at a pyrrole nitrogen and also the number of carboxylic acid side chains of the substituted porphyrin are important for the inhibitory effect. Evidence that N-methyl mesoporphyrin inhibited the enzyme, whereas the ethylene-derived pigment did not, was also obtained in vivo.

MeSH terms

  • 5-Aminolevulinate Synthetase / metabolism
  • Animals
  • Coproporphyrins / chemical synthesis
  • Coproporphyrins / metabolism
  • Coproporphyrins / pharmacology*
  • Ferrochelatase / antagonists & inhibitors*
  • Liver / metabolism
  • Lyases / antagonists & inhibitors*
  • Male
  • Mesoporphyrins / chemical synthesis
  • Mesoporphyrins / metabolism
  • Mesoporphyrins / pharmacology*
  • Mice
  • Pigments, Biological / pharmacology
  • Porphyrins / pharmacology*
  • Spectrophotometry
  • Structure-Activity Relationship

Substances

  • Coproporphyrins
  • Mesoporphyrins
  • Pigments, Biological
  • Porphyrins
  • N-ethyl mesoporphyrin
  • N-methyl coproporphyrin
  • 5-Aminolevulinate Synthetase
  • Lyases
  • Ferrochelatase