Abstract
Senescent chloroplasts (gerontoplasts) isolated from primary leaves of barley (Hordeum vulgare L.) contained a group of fluorescent chlorophyll (Chl) compounds designated as FCC-2, FCC-3 and FCC-4. Compound FCC-2 represents an established catabolite of Chl-porphyrin and was the most abundant constituent of this group. One of the minor constituents, FCC-4, was produced in a reconstituted system composed of thylakoids and stroma. The generation of FCC-4 depended on oxygen and required reduced ferredoxin (Fd) which probably acts as a reductant of the putative oxygenating enzyme responsible for the cleavage of Chl-porphyrin. A typical assay mixture consisted of thylakoids and stroma (equalling 108 gerontoplasts), Fd, NADPH and glucose-6-phosphate for NADPH-regeneration. The oxygenating enzyme appeared to be a stromal protein. However, enzyme activities associated with the thylakoids were also required for the production of FCC-4. The senescence-specific part of the reconstituted system resided in the thylakoids. Thus, FCC-4 was produced in assay mixtures of senescent thylakoids and stroma from presenescent chloroplasts, whereas combinations with presenescent thylakoids failed to yield appreciable amounts of this putative primary Chl-catabolite.
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Abbreviations
- Chl:
-
chlorophyll
- FCC:
-
fluorescent chlorophyll catabolite
- Fd:
-
ferredoxin
- Glc6P:
-
glucose-6-phosphate
References
Allen, J.F. (1975) A two-step mechanism for the photosynthetic reduction of oxygen by ferredoxin. Biochem. Biophys. Res. Commun. 66, 36–43
Bortlik, K., Peisker, C., Matile, Ph. (1990) A novel type of chlorophyll catabolite in senescent barley leaves. J. Plant Physiol. 136, 161–165
Düggelin, T., Schellenberg, M., Bortlik, K., Matile, Ph. (1988) Vacuolar location of lipofuscin- and proline-like compounds in senescent barley leaves. J. Plant Physiol. 133, 492–497
Engel, N., Jenny, T.A., Mooser, V., Gossauer, A. (1991) Chlorophyll catabolism in Chlorella protothecoides. Isolation and structure elucidation of a red bilin derivative. FEBS Lett. 293, 1–133
Ginsburg, S., Matile, Ph. (1993) Identification of catabolites of chlorophyll-porphyrin in senescent rape cotyledons. Plant Physiol., in press
Kräutler, B., Jaun, B., Bortlik, K., Schellenberg, M., Matile, Ph. (1991) On the enigma of chlorophyll degradation: the constitution of a secoporphinoid catabolite. Angew. Chem. Int. Ed. Engl. 30, 1315–1318
Kräutler, B., Jaun, B., Amrein, W., Bortlik, K., Schellenberg, M., Matile, Ph. (1992) Breakdown of chlorophyll: constitution of a secoporphinoid chlorophyll catabolite isolated from senescent barley leaves. Plant Physiol. Biochem. 30, 333–346
Matile, Ph., Schellenberg, M., Peisker, C. (1992) Production and release of a chlorophyll catabolite in isolated senescent chloroplasts. Planta 187, 230–235
Peisker, C., Thomas, H., Keller, F., Matile, Ph. (1990) Radiolabelling of chlorophyll for studies of catabolites. J. Plant Physiol. 136, 544–549
Schellenberg, M., Matile, Ph., Thomas, H. (1990) Breakdown of chlorophyll in chloroplasts of senescent barley leaves depends on ATP. J. Plant. Physiol. 136, 564–568
Shin, M. (1971) Ferredoxin-NADP reductase from spinach. Methods Enzymol. 23, 440–447
Schoch, S., Brown, J. (1987) The action of chlorophyllase on chlorophyll-protein complexes. J. Plant Physiol. 126, 483–494
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The authors are indebted to the Swiss National Science Foundation for financial support and to E. Disler for help with the manuscript.
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Schellenberg, M., Matile, P. & Thomas, H. Production of a presumptive chlorophyll catabolite in vitro: requirement for reduced ferredoxin. Planta 191, 417–420 (1993). https://doi.org/10.1007/BF00195702
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DOI: https://doi.org/10.1007/BF00195702