Interactions of herbicides and azidoquinones at a Photosystem II binding site in the thylakoid membrane

Willem Vermaas, Charles J. Arntzen, L. Q. Gu, C. A. Yu

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

6-Azido-5-decyl-2,3-dimethoxy-p-benzoquinone (6-azido-Q0C10) was found to replace the native plastoquinone at B (the second stable electron acceptor to Photosystem II (PS II)). The 6-azido-Q10C10 would accept electrons from the primary electron-accepting quinone, Q, thus allowing electron transport through PS II to the plastoquinone pool in thylakoids. The synthetic azidoquinone also competes with the PS II herbicides ioxynil and atrazine for binding. This observation strongly favors the hypothesis that PS II herbicides block electron transport by replacing the native quinone which acts as the second electron carrier on the reducing side of PS II (termed B). Covalent linkage of 6-azido-Q0C10 to its binding environment by ultraviolet irradiation greatly reduces herbicide-binding affinity but does not lead to a loss in herbicide-binding sites. We take this as evidence that covalent attachment of 6-azido-Q0C10 allows some freedom of quinone head-group movement such that the herbicides can enter the binding site. This indicates that the protein determinants which regulate quinone and herbicide binding are very closely related, but not identical. A compound somewhat related to 6-azido-Q0C10 is 2-azido-3-methoxy-5-geranyl-6-methyl-p-benzoquinone (2-azido-Q2). This compound was found to be an ineffective competitor with respect to herbicide binding. Thus, interactions with protein-binding determinants are highly dependent on the molecular structure of quinones. The 2-azido-Q2 was an inhibitor of electron flow in the intersystem portion of the chain.

Original languageEnglish (US)
Pages (from-to)266-275
Number of pages10
JournalBBA - Bioenergetics
Volume723
Issue number2
DOIs
StatePublished - May 27 1983
Externally publishedYes

Fingerprint

Thylakoids
Photosystem II Protein Complex
Herbicides
Binding Sites
Membranes
Electrons
Plastoquinone
Electron Transport
Atrazine
Quinones
Head Movements
Molecular Structure
Protein Binding
Molecular structure
benzoquinone
Irradiation

Keywords

  • (Pea chloroplast)
  • Azidoquinone
  • Herbicide
  • Photosynthesis
  • Photosystem II
  • Thylakoid membrane

ASJC Scopus subject areas

  • Biophysics

Cite this

Interactions of herbicides and azidoquinones at a Photosystem II binding site in the thylakoid membrane. / Vermaas, Willem; Arntzen, Charles J.; Gu, L. Q.; Yu, C. A.

In: BBA - Bioenergetics, Vol. 723, No. 2, 27.05.1983, p. 266-275.

Research output: Contribution to journalArticle

Vermaas, Willem ; Arntzen, Charles J. ; Gu, L. Q. ; Yu, C. A. / Interactions of herbicides and azidoquinones at a Photosystem II binding site in the thylakoid membrane. In: BBA - Bioenergetics. 1983 ; Vol. 723, No. 2. pp. 266-275.
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AB - 6-Azido-5-decyl-2,3-dimethoxy-p-benzoquinone (6-azido-Q0C10) was found to replace the native plastoquinone at B (the second stable electron acceptor to Photosystem II (PS II)). The 6-azido-Q10C10 would accept electrons from the primary electron-accepting quinone, Q, thus allowing electron transport through PS II to the plastoquinone pool in thylakoids. The synthetic azidoquinone also competes with the PS II herbicides ioxynil and atrazine for binding. This observation strongly favors the hypothesis that PS II herbicides block electron transport by replacing the native quinone which acts as the second electron carrier on the reducing side of PS II (termed B). Covalent linkage of 6-azido-Q0C10 to its binding environment by ultraviolet irradiation greatly reduces herbicide-binding affinity but does not lead to a loss in herbicide-binding sites. We take this as evidence that covalent attachment of 6-azido-Q0C10 allows some freedom of quinone head-group movement such that the herbicides can enter the binding site. This indicates that the protein determinants which regulate quinone and herbicide binding are very closely related, but not identical. A compound somewhat related to 6-azido-Q0C10 is 2-azido-3-methoxy-5-geranyl-6-methyl-p-benzoquinone (2-azido-Q2). This compound was found to be an ineffective competitor with respect to herbicide binding. Thus, interactions with protein-binding determinants are highly dependent on the molecular structure of quinones. The 2-azido-Q2 was an inhibitor of electron flow in the intersystem portion of the chain.

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