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. 1987 Jun;84(2):348-52.
doi: 10.1104/pp.84.2.348.

Degradation of the 32 kD Herbicide Binding Protein in Far Red Light

V Gaba  1 , J B Marder, B M Greenberg, A K Mattoo, M Edelman
Affiliations

Degradation of the 32 kD Herbicide Binding Protein in Far Red Light

V Gaba et al. Plant Physiol. 1987 Jun.

Abstract

White light (400-700 nanometers) supports the activity of photosystem I (PSI) and photosystem II while far red light (>/=700 nanometers) supports PSI almost exclusively. In intact fronds of Spirodela oligorrhiza, turnover of the 32 kilodaltons herbicide binding protein is stimulated under both these light conditions, although not in the dark or at wavelengths >730 nanometers. As is the case in white light, the far red light induced degradation of the protein is inhibited by DCMU. The means by which far red light operates is unclear. Hypotheses considered include: PSI activated proteolysis, PSI-induced formation of semiquinone anions, and PSI-generated free radicals.

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