Abstract
Binding of the 4-azido analog of the herbicide atrazine to pea chloroplast membranes was compared with that of atrazine. When [14C]azidoatrazine was treated with 300-nanometer ultraviolet light in situ, reversibility of binding was lost in proportion to the duration of irradiation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of chloroplast membranes irradiated in the presence of [14C]azidoatrazine indicated radioactivity in only one region, corresponding to a protein with a molecular weight of approximately 32,000. Azidoatrazine is a photoaffinity reagent for the triazine binding site in chloroplasts and serves as a label to identify this site, which may be the apoprotein of the secondary electron acceptor in photosystem II.
Original language | English (US) |
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Pages (from-to) | 937-940 |
Number of pages | 4 |
Journal | Science |
Volume | 211 |
Issue number | 4485 |
DOIs | |
State | Published - 1981 |