Inhibition of zeaxanthin epoxidase activity by cadmium ions in higher plants.
The effect of cadmium and zinc ions on violaxanthin cycle enzymes, violaxanthin de-epoxidase and zeaxanthin epoxidase, has been investigated on selected plant species, as well as in vitro. About 50% inhibition of zeaxanthin epoxidase by cadmium ions was found for duckweed (Lemna trisulca) and tomato (Lycopersicon esculentum) leaves but for apricot (Prunus armeniaca) leaves no cadmium inhibition of the epoxidation reaction was observed. The cadmium inhibition of zeaxanthin epoxidase in tomato was abolished by zinc ions. Zinc ions alone did not affect the activity of neither of the enzymes of the violaxanthin cycle. This suggests that mechanism of cadmium inactivation of the enzyme relies on cadmium interaction with a cysteine residue of the protein, important for the enzyme activity. The target cysteine in tomato epoxidase could be the cysteine residue present in the most conservative part of the molecule which is not present in the apricot enzyme sequence. Neither stimulation nor inhibition of violaxanthin de-epoxidase by cadmium ions both in vivo and in vitro studies was detected. It confirms the proposed mechanism of zeaxanthin epoxidation inhibition by cadmium ions because the cysteine residue in the conservative motif of violaxathin de-epoxidase is not present.
Latowski
Dariusz
D
Department of Chemistry, Pedagogical University, ul. Podchorazych 2, 30-084 Kraków, Poland. latowski@interia.pl
Kruk
Jerzy
J
Strzałka
Kazimierz
K
D029064:Araceae / Q000737:chemistry / Q000201:enzymology; D002104:Cadmium / Q000494:pharmacology / Q000633:toxicity*; D003545:Cysteine / Q000737:chemistry; D007477:Ions; D018551:Solanum lycopersicum / Q000737:chemistry / Q000201:enzymology; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D027861:Prunus / Q000737:chemistry / Q000201:enzymology
D007477:Ions; D002104:Cadmium; D010088:Oxidoreductases; C097153:zeaxanthin epoxidase; D003545:Cysteine