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PMID: 8503883 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Investigation of the subcellular location of the tetrapyrrole-biosynthesis enzyme coproporphyrinogen oxidase in higher plants.

The Biochemical journal ·Vol. 292 ( Pt 2) ·1993-06-01 ·Pages 503-8

Smith AG, Marsh O, Elder GH

Abstract

The subcellular location of two enzymes in the biosynthetic pathway for protoporphyrin IX, coproporphyrinogen (coprogen) oxidase (EC 1.3.3.3) and protoporphyrinogen (protogen) oxidase (EC 1.3.3.4) has been investigated in etiolated pea (Pisum sativum) leaves and spadices of cuckoo-pint (Arum maculatum). Plant tissue homogenized in isotonic buffer was subjected to subcellular fractionation to prepare mitochondria and plastids essentially free of contamination by other cellular organelles, as determined by marker enzymes. Protogen oxidase activity measured fluorimetrically was reproducibly found in both mitochondria and etioplasts. In contrast, coprogen oxidase could be detected only in etioplasts, using either a coupled fluorimetric assay or a sensitive radiochemical method. The implications of these results for the synthesis of mitochondrial haem in plants is discussed.

MeSH Terms
Cell Fractionation Coproporphyrinogen Oxidase/metabolism Fabaceae/enzymology Organelles/enzymology Oxidoreductases/metabolism Oxidoreductases Acting on CH-CH Group Donors Plants, Medicinal Protoporphyrinogen Oxidase Pyrroles/metabolism Tetrapyrroles
Chemicals
Pyrroles Tetrapyrroles Oxidoreductases Oxidoreductases Acting on CH-CH Group Donors Coproporphyrinogen Oxidase Protoporphyrinogen Oxidase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Smith A G
Department of Plant Sciences, University of Cambridge, U.K.
Marsh O
Elder G H
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1993-06-01
Pages
503-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1134238
Subset
IM
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