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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1984 Oct;81(20):6310–6314. doi: 10.1073/pnas.81.20.6310

Triazine herbicide resistance in the photosynthetic bacterium Rhodopseudomonas sphaeroides

Alfred E Brown *, Carl W Gilbert , Rachel Guy , Charles J Arntzen
PMCID: PMC391913  PMID: 16593520

Abstract

The photoaffinity herbicide azidoatrazine (2-azido-4-ethylamino-6-isopropylamino-s-triazine) selectively labels the L subunit of the reaction center of the photosynthetic bacterium Rhodopseudomonas sphaeroides. Herbicide-resistant mutants retain the L subunit and have altered binding properties for methylthio- and chloro-substituted triazines as well as altered equilibrium constants for electron transfer between primary and secondary electron acceptors. We suggest that a subtle alteration in the L subunit is responsible for herbicide resistance and that the L subunit is the functional analog of the 32-kDa QB protein of chloroplast membranes.

Keywords: bacterial reaction centers, herbicide-binding protein, photosynthesis, membrane proteins, atrazine

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Selected References

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