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 Citations (Scopus)

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
Externally publishedYes

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Biliverdine
Heme Oxygenase (Decyclizing)
Heme
Degradation
Methemalbumin
NADPH-Ferrihemoprotein Reductase
Isomers
Myoglobin
High performance liquid chromatography
High Pressure Liquid Chromatography
Chemical analysis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Heme oxygenase provides α-selectivity to physiological heme degradation. / Docherty, John C.; Masters, Bettie Sue Siler; Firneisz, Gay D.; Schacter, Brent A.

In: Biochemical and Biophysical Research Communications, Vol. 105, No. 3, 14.04.1982, p. 1005-1013.

Research output: Contribution to journalArticle

Docherty, John C. ; Masters, Bettie Sue Siler ; Firneisz, Gay D. ; Schacter, Brent A. / Heme oxygenase provides α-selectivity to physiological heme degradation. In: Biochemical and Biophysical Research Communications. 1982 ; Vol. 105, No. 3. pp. 1005-1013.
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