Abstract
AbstractThe inhibition of the oxygen evolution rate (OER) in Chlorella vulgaris by 2-alkylsulphanyl-4-pyridinecarbothioamides (APCTs; alkyl = methyl up to hexadecyl) was studied. APCTs were found to inhibit photosynthetic electron transport (PET) which resulted in the inhibition of OER in algae. The inhibitory activity of APCTs was highly dependent on the alkyl chain length of the 2-alkylsulphanyl substituent and the corresponding dependence showed a bilinear course with the decyl derivative as being the most active inhibitor. Using EPR spectroscopy, the site of APCT action in the algal photosynthetic apparatus was determined. It was confirmed that APCT interacted mainly with the D. intermediate, i.e. with tyrosine radical (TyrD) occurring at the 161st position in D2 protein which is situated on the donor side of photosystem 2.
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