Heme oxygenase provides α-selectivity to physiological heme degradation

John C. Docherty, Bettie Sue Siler Masters, Gay D. Firneisz, Brent A. Schacter

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

The isomeric composition of biliverdin formed by the degradation of heme by purified NADPH-cytochrome c reductase has been determined by high performance liquid chromatography. Methemalbumin heme yields a mixture of the four biliverdin IX isomers while myoglobin yields only the IX-α isomer of biliverdin. In both cases biliverdin is a minor product of the reaction. Addition of purified heme oxygenase to the methemalbumin NADPH-cytochrome c reductase system confers α-selectivity on the reaction and allows stoichiometric conversion of heme to biliverdin. Thus the role of heme oxygenase in enzymatic heme degradation appears to be to provide a suitable environment for quantitative conversion of heme to biliverdin in addition to conferring α-selectivity on the reaction.

Original languageEnglish (US)
Pages (from-to)1005-1013
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume105
Issue number3
DOIs
StatePublished - Apr 14 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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