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Destruction of cytochrome P-450 by ethylene. Structure of the resulting prosthetic heme adduct.

Authors
  • Ortiz de Montellano, P R
  • Beilan, H S
  • Kunze, K L
  • Mico, B A
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
May 10, 1981
Volume
256
Issue
9
Pages
4395–4399
Identifiers
PMID: 7217086
Source
Medline
License
Unknown

Abstract

The prosthetic heme of cytochrome P-450 is converted during the metabolism of ethylene into an abnormal hepatic porphyrin. This porphyrin has been isolated, purified, and characterized by field desorption mass spectrometry and 360-MHz nuclear magnetic resonance spectroscopy. It has been unambiguously identified as one of the four possible isomers of N-(2-hydroxyethyl)protoporphyrin IX (isolated as the dimethyl ester). The isomer which is obtained bears the N-alkyl group on one of the two propionic acid-substituted pyrrole rings in the porphyrin. Strong support is provided by the structure of this porphyrin for our contention that the prosthetic heme of cytochrome P-450 is alkylated during attempted transfer of the catalytically-activated oxygen to the pi-bond of destructive unsaturated substrates.

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