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. 1976 Jul;58(1):43-6.
doi: 10.1104/pp.58.1.43.

Enzymic nature of the protein moiety of protochlorophyllide holochrome

Y Manetas  1 , G A Akoyunoglou
Affiliations

Enzymic nature of the protein moiety of protochlorophyllide holochrome

Y Manetas et al. Plant Physiol. 1976 Jul.

Abstract

The enzymic nature of the protein moiety of protochlorophyll(ide) holochrome was studied by following the fate of the [(14)C]protochlorophyll(ide) formed when dark-grown barley (Hordeum vulgare) or bean (Phaseolus vulgaris) leaves are incubated in the dark with 3 mm 4-delta-[(14)C]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 delta-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.

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References

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    1. Plant Physiol. 1967 Jun;42(6):781-4 - PubMed
    1. Plant Physiol. 1970 Aug;46(2):240-6 - PubMed
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