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) |
|---|---|
| Pages (from-to) | 937-940 |
| Number of pages | 4 |
| Journal | Science |
| Volume | 211 |
| Issue number | 4485 |
| DOIs | |
| State | Published - 1981 |