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Enzymic Nature of the Protein Moiety of Protochlorophyllide Holochrome

^a Department of Biology, Nuclear Research Center "Demokritos," Athens, Greece

The enzymic nature of the protein moiety of protochlorophyll(ide) holochrome was studied by following the fate of the [¹⁴C]protochlorophyll(ide) formed when dark-grown barley (Hordeum vulgare) or bean (Phaseolus vulgaris) leaves are incubated in the dark with 3 mM 4--[¹⁴C]aminolevulinic acid. It was found that: [List: see text]

Since turnover of protochlorophyll(ide) was not observed, these results show that there is a free exchange between the old "endogenous" and the new -aminolevulinic-acid-induced protochlorophyll(ide) molecules on the active site of the holochrome protein. These results are consistent with the hypothesis that the holochrome protein acts as an enzyme.