Rat liver cytochrome P-450b, P-420b, and P-420c are degraded to biliverdin by heme oxygenase.

Abstract:

:In this report we provide data, for the first time, demonstrating the conversion of the heme moiety of certain cytochrome P-450 and P-420 preparations, to biliverdin, catalyzed by heme oxygenase. We have used purified preparations of cytochromes P-450c, P-450b, P-450/P-420c, or P-450/P-420b as substrates in a heme oxygenase assay system reconstituted with heme oxygenase isoforms, HO-2 or HO-1, NADPH-cytochrome c (P-450) reductase, biliverdin reductase, NADPH, and Emulgen 911. With cytochrome P-450b or P-450/P-420b preparations, a near quantitative conversion of degraded heme to bile pigments was observed. In the case of cytochrome P-450/P-420c approximately 70% of the degraded heme was accounted for as bilirubin but only cytochrome P-420c was appreciably degraded. The role of heme oxygenase in this reaction was supported by the following observations: (i) bilirubin formation was not observed when heme oxygenase was omitted from the assay system; (ii) the rate of degradation of the heme moiety was at least threefold greater with heme oxygenase and NADPH-cytochrome c (P-450) reductase than that observed with reductase alone; and (iii) the presence of Zn- or Sn-protoporphyrins (2 microM), known competitive inhibitors of heme oxygenase, resulted in 70-90% inhibition of bilirubin formation.

journal_name

Arch Biochem Biophys

authors

Kutty RK,Daniel RF,Ryan DE,Levin W,Maines MD

doi

10.1016/0003-9861(88)90492-4

subject

Has Abstract

pub_date

1988-02-01 00:00:00

pages

638-44

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90492-4

journal_volume

260

pub_type

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