Abstract
A soluble protein-chlorophyll complex was isolated from spinach chloroplasts by extraction with Triton X-100 and chromatography on DEADE-cellulose in the presence of 0.05% Triton X-100. The complex was able to photorduced ferricyanide at rates 10–% of those of whole chloroplast, but was unable to reduce either dichlorophenolindophenol or NADP. No photosynthetic ATP formation could be detected, but a slow photohydrolysis of ATP was observed. Evidence for the inhibition of ferricyanide reduction by sulfhydryl groups on the complex is presented.
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