Non-enzymic nature of the pyridine haemochrome-cleaving activity of mammalian tissue extracts (‘haem α-methyl oxygenase’)

Author:

Colleran Emer1,Carra P. Ó1

Affiliation:

1. Department of Biochemistry, University College, Galway, Irish Republic

Abstract

1. The pyridine haemochrome-cleaving activity of extracts from mammalian liver and other tissues is shown conclusively to be entirely non-enzymic in nature and attributable to coupled oxidation with ascorbate. 2. Reduced glutathione probably contributes to the activity indirectly by continuously regenerating the ascorbate to the reduced form. 3. The cleavage shows no specificity for the α-methine bridge of pyridine haemochrome. 4. Results are presented suggesting some probable reasons for the erroneous characterization of the activity as an α-methine-specific haem-cleaving enzyme (`haem α-methenyl oxygenase') by Nakajima and co-workers (e.g. Nakajima, Takemura, Nakajima & Yamaoka, 1963; Nakajima & Gray, 1967).

Publisher

Portland Press Ltd.

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1. Hemes, Chlorophylls, and Related Compounds: Biosynthesis and Metabolic Regulation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

2. Detection of Biliverdin Reductase Activity;Current Protocols in Toxicology;1999-05

3. Purification and Properties of Cow Splenic Biliverdin Reductase;Preparative Biochemistry;1994-11

4. Methene bridge carbon atom elimination in oxidative heme degradation catalyzed by heme oxygenase and NADPH-cytochrome P-450 reductase;Archives of Biochemistry and Biophysics;1984-12

5. Iron Metabolism;Physiology;1984

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