NDLI: The Ethylene-Induced Chlorophyll Catabolism of Radish (Raphanus sativus L.) Cotyledons : Production of Colorless Fluorescent Chlorophyll Catabolite (FCC) In vitro

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The Ethylene-Induced Chlorophyll Catabolism of Radish (Raphanus sativus L.) Cotyledons : Production of Colorless Fluorescent Chlorophyll Catabolite (FCC) In vitro

Content Provider	Semantic Scholar
Author	Adachi, Masaru Nakabayashi, Kenichi Azuma, Rie Kurata, Hirofumi Takahashi, Yoshihiro Shimokawa, Keishi
Copyright Year	1999
Abstract	Ethylene enhanced the degreening and increased the chlorophyll (Chl)-oxidative enzyme activity in intact radish (Raphanus sativus L.)(Rs) cotyledons kept in the dark. The catabolism of Chl α-porphyrin in plants was investigated by using crude proteins from ethylene-induced degreening radish cotyledons. The enzyme catalyzes the degradation of Chl α in the presence of H2O2 and 2, 4-dichlorophenol (DCP), or p-coumaric acid. Analysis by HPLC and HPTLC revealed the appearance of C-132-hydroxy (HO)Chl α. The reaction of C-132-HO Chl α formation was inhibited completely by ascorbate (2mM) or KCN (2mM), but it was not under an anoxygenic condition. These results suggest that C-132-HO Chl α forming enzyme is aperoxygenase and/or peroxygenase-like peroxidase, the peroxidase-catalyzed oxygen transfer from H2O2. Moreover, the 3-dimensional (3-D) fluorescence spectral measurements showed that a colorless fluorescent Chl catabolite (FCC : Ex 350 nm/Em 455 nm) was produced with a concomitant decrease in Chl α level. The production of C-132-HO Chl α and colorless Rs-FCC was inhibited by heating the extracts. It appears that Chl α-porphyrin is catabolized by the proteins prepared from Raphanus sativus cotyledons via the following reaction : Chl α→C-132-HO Chl α→→colorless Rs-FCC (Chl-porphyrin oxygenolytic cleavage catabolite).
Starting Page	1139
Ending Page	1145
Page Count	7
File Format	PDF HTM / HTML
DOI	10.2503/jjshs.68.1139
Volume Number	68
Alternate Webpage(s)	http://dl.ndl.go.jp/view/download/digidepo_10469609_po_ART0001964328.pdf?alternativeNo=&contentNo=1
Alternate Webpage(s)	https://doi.org/10.2503/jjshs.68.1139
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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