Protoporphyrinogen-IX oxidase inhibitors: Bioactivation of thiadiazolidines

Pesticide Biochemistry and Physiology

Volumn 70, Issue 3, 2001, Pages 159-167

  Hiraki, Masaki ^a   Ohki, Shinpei ^a   Sato, Yukiharu ^a   Jablonkai, Istvan ^b   Böger, Peter ^c   Wakabayashi, Ko ^a  

^a TAMAGAWA UNIVERSITY   (Japan)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^c UNIVERSITY OF KONSTANZ   (Germany)

Author keywords

Bioactivation; Glutathione S transferase; SH compounds; Thiadiazolidines; Thiol intermediate; Thiosemicarbazides; Triazolidines

Indexed keywords

SCENEDESMUS ACUTUS; ZEA MAYS;

EID: 0034813531     PISSN: 00483575     EISSN: None     Source Type: Journal    
DOI: 10.1006/pest.2001.2552     Document Type: Article

References (12)

1. General physiological characteristics and mode of action of peroxidizing herbicides
2. Isomerization and peroxidizing phytotoxicity of thiadiazolidine-thione compounds
3. Isomerization and peroxidizing phytotoxicity of thiadiazolidine herbicides
4. Enzymatic conversion of thiadiazolidine-type peroxidizing herbicides into more active triazolidines
5. A novel isourazole herbicide, fluthiacet-methyl, is a potent inhibitor of protoporphyrinogen oxidase after isomerization by glutathione S-transferase
6. Enzyme-modified phytotoxic structure of thiadiazolidine compounds
7. Isomerization of peroxidizing thiadiazolidine herbicides is catalyzed by glutathione S-transferase
8. Chemical catalysis of the isomerization of peroxidizing herbicidal thiadiazolidines
9. Peroxidizing phytotoxic activity of thiadiazolidine and triazolidine compounds
10. Inhibition of protoporphyrinogen oxidase from maize
11. Quantitative correlation between short-term accumulation of protoporphyrin IX and peroxidative activity of cyclic imides
12. Metabolic modification of isoimide type peroxidizing compounds catalyzed by an isoenzyme