Evidence for a monooxygenase-catalyzed primary process in the catabolism of chlorophyll

Only recently have products of the enzymatic breakdown of the chlorophylls been characterized for the first time. All catabolites isolated until now from a chlorophyte and from angiosperms have in common the position at which the primary oxygenative ring cleavage occurs, yielding linear tetrapyrrole...

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Bibliographic Details
Published in:FEBS letters 1995-05, Vol.364 (1), p.41-44
Main Authors: Curty, Christophe, Engel, Norbert, Gossauer, Albert
Format: Article
Language:English
Subjects:
18O labeling
19-Formyl-1[21H,22H]bilinone
Chlorella - enzymology
Chlorella protothecoides
Chlorophyll - analogs & derivatives
Chlorophyll - metabolism
Chlorophyll catabolism
Mass Spectrometry
Models, Biological
Monooxygenase
Oxygen - metabolism
Oxygenases - metabolism
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Summary:Only recently have products of the enzymatic breakdown of the chlorophylls been characterized for the first time. All catabolites isolated until now from a chlorophyte and from angiosperms have in common the position at which the primary oxygenative ring cleavage occurs, yielding linear tetrapyrroles (19-formyl-1[21H,22H]bilinones). In vivo studies of 18,18O 2 incorporation in one of the chlorophyll catabolites isolated from Chlorella protothecoides show unequivocally that of the two oxygen atoms inserted into the pigment, only the formyl oxygen originates from dioxygen whereas the other one, the lactamic oxygen atom, derives from water. These findings suggest a monooxygenase-catalyzed primary process in the catabolism of chlorophyll.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00348-D