Add time:09/08/2019         Source:sciencedirect.com

Phenmedipham strongly inhibits the electron transfer through PSII (50% inhibition at 0.02 μM). Its affinity for thylakoids is high (Km = 0.137 μM). A Km value of 0.067μM could be estimated for its specific binding to the D-1 protein. Diuron could replace phenmedipham on this target for which saturation was obtained at 2 nmol mg−1 chlorophyll. In class A chloroplasts, the amount of phenmedipham needed to obtain a target saturation is much higher, showing that a large proportion of the herbicide (140% of the amount retained by thylakoids) remains associated with the nonthylakoidal components of the chloroplasts, probably the envelope. When increasing the phenmedipham concentration, the amount associated with thylakoids increases markedly, showing that a great part of the product may either be trapped by the lipids or adsorbed on the lipophilic sites of the thylakoid surface or both. A very similar process is seen with purified mitochondria. Furthermore, at 50 to 60 nmol mg−1 protein, phenmedipham induces a full and selective inhibition of the external NADH dehydrogenase of the inner mitochondrial membrane. The high lipophilicity of phenmedipham can probably explain, at least for one part, that it greatly concentrates inside the different types of biological membranes. Such a large membrane concentration seems not to occur with other well-known PSII inhibitors. This observation could contribute to explain why phenmedipham can be efficient through foliar treatment under field conditions.

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