Evidence for a Dual Function of the Herbicide-Binding D1 Protein in Photosystem II

James G. Metz, Himadri B. Pakrasi, Michael Seibert, Charles J. Arntzer

Research output: Contribution to journalArticlepeer-review

117 Scopus Citations


The LF-1 mutant of the green alga Scenedesmus obliquus is completely blocked on the oxidizing (water-splitting) side of photosystem II (PS II) while the reaction center and reducing side remain functional. A 34-kDa protein found in the PS II reaction center core complex of wild-type cells is replaced by a 36-kDa protein in the mutant cells. Both of these proteins are labeled by azido[14C]atrazine and are recognized by polyclonal antibodies raised against the herbicide-binding, D1 protein of Amaranthus hybridus. The data provide a new perspective on the role of the D1 protein by implying that it affects the oxidizing side of PS II in addition to performing its well established function on the reducing side.

Original languageAmerican English
Pages (from-to)269-274
Number of pages6
JournalFEBS Letters
Issue number2
StatePublished - 1986

Bibliographical note

Work performed by Photoconversion Research Branch, Solar Energy Research Institute, Golden, Colorado and Central Research & Development Department, E. I. DuPont de Nemours and Co., Wilmington, Delaware

NREL Publication Number

  • ACNR/JA-233-7965


  • Azidoatrazine Herbicide binding Photosystem II Oxygen evolution (Scenedesmus
  • LF-1 mutant)


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