Chlorophyll catabolism in <i>Chlorella protothecoides</i> Isolation and structure elucidation of a red bilin derivative

Engel, Norbert; Jenny, Titus A.; Mooser, Véronique; Gossauer, Albert

doi:10.1016/0014-5793(91)81168-8

Cited by 109 publications

(79 citation statements)

References 18 publications

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“…The same selectivity was also found in the red bilin from Chlorella protothecoides (Engel et al, 1991(Engel et al, , 1996, but another mechanism seems to be responsible for breakdown of Chl into the luciferin of the dinoflagellate Pyrocystis lunula, which is oxygenolytically cleaved at the C20/C1 mesoposition (Nakamura et al, 1989).…”

Section: Discussionmentioning

confidence: 52%

Chlorophyll Breakdown in Senescent Chloroplasts (Cleavage of Pheophorbide a in Two Enzymic Steps)

et al. 1997

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Section: Discussionmentioning

confidence: 52%

Chlorophyll Breakdown in Senescent Chloroplasts (Cleavage of Pheophorbide a in Two Enzymic Steps)

et al. 1997

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“…The occurrence of this type of catabolite has been associated with Chl breakdown in higher plants (Bortlik et al, 1990;Krautler et al, 1991) and in a green alga (Engel et al, 1991). This may indicate the existence of a common enzymic mechanism of Chl breakdown.…”

Section: Properties Of Chl Catabolitesmentioning

confidence: 84%

“…Unexpected features of RP 14 include the hydroxylations in both vinyl and ethyl side chains of pyrroles A and B as well as the preservation of the carboxy-methylester in the isocyclic ring. The constitution of a similar linear tetrapyrrole isolated from Chlorella protothecoides (Engel et al, 1991) suggests that ring cleavage in the a-position also occurs in green algae. In contrast, a catabolite of Chl that acts as light emitter in a bioluminescent dinoflagellate is cleaved in the 6-position between pyrroles A and D, whereby the carbon atom of the methine bridge is lost (Nakamura et al, 1988(Nakamura et al, , 1989.…”

mentioning

confidence: 99%

Identification of Catabolites of Chlorophyll-Porphyrin in Senescent Rape Cotyledons

Ginsburg

Matile

1993

Plant Physiol.

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Developing shoots of rape seedlings (Brassica napus 1.) were excised and fed with 4-['4C]5-aminolevulinic acid to label the pyrroles in chlorophyll (Chl) synthesized during the final phase of expansion and greening of the cotyledons. About 80% of 14C taken up into the cotyledons was incorporated into Chl. The subsequent incubation of labeled shoots in permanent darkness caused the rapid loss of labeled Chl while increasing proportions of 14C appeared in the fradion of water-soluble compounds. Reversedphase high performance liquid chromatography resolved three nonfluorescent polar catabolites of Chl-porphyrin that were progressively accumulated as senescence advanced. At intermediate stages of senescence, the cotyledons contained a fluorescent radioadive derivative of Chl that was also detectable, together with traces of other putative fluorescent catabolites, in isolated senescent chloroplasts. l h e nonfluorescent catabolites, identified by means of radiolabeling, were also found to accumulate in attached cotyledons senescing under photoperiod; under these conditions, one of the compounds, NCC-1, was particularly abundant. The catabolites of rape exhibited the same ultraviolet spedra, characterized by a maximum at 320 nm, as a previously reported seco-

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“…Structure of Chi catabolites published so far point to the existence of a common mechanism of oxygenolytic opening of the chlorin-macrocycle (Engel et al, 1991;Krautler et al, 1991Krautler et al, , 1992Muhlecker et al 1993;Itturaspe, Engel & Gossauer, 1994). Thus, cleavage of Chl-porphyrin can formally be described as the addition of molecular oxygen to the double bond in C-4/C-5 mesoposition between pyrroles A and B (Ginsburg et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Chlorophyll breakdown in senescent cotyledons of rape, Brassica napus L.: Enzymatic cleavage of phaeophorbide a in vitro

1995

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SUMMARYSolubilization of senescent thylakoids from rape cotyledons in the presence of Triton X-100 was employed to establish an in vitro system that allowed the assessment of enzymatic conversion of phaeophorbide a into an uncoloured fluorescent chlorophyll catabolite, Bn-FCC-2. The action of the putative dioxygenase responsible for the cleavage of the porphyrin macrocycle depends on reduced ferredoxin as reductant. Apart from this thylakoidal catalyst, stromal protein is also required for the production of FCC-2 in vitro. The cleavage reaction does not occur with phaeophorbide b as substrate. Saturation kinetics with phaeophorbide a as substrate yielded an apparent K^-value of c. 200 //M. The enzyme contains iron as suggested by inhibitory effects of appropriate chelators. Enzyme activity lost upon treatment with bipyridyl was partly restored in the presence of Fe-ions; other metal ions such as Cu, Zn and Co were ineffective. The enzyme is absent in the thylakoids of mature green cotyledons. It appears upon the induction of foliar senescence and reaches the highest levels towards the end of the yellowing process.

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Chlorophyll catabolism in Chlorella protothecoides Isolation and structure elucidation of a red bilin derivative

Cited by 109 publications

References 18 publications

Chlorophyll Breakdown in Senescent Chloroplasts (Cleavage of Pheophorbide a in Two Enzymic Steps)

Chlorophyll Breakdown in Senescent Chloroplasts (Cleavage of Pheophorbide a in Two Enzymic Steps)

Identification of Catabolites of Chlorophyll-Porphyrin in Senescent Rape Cotyledons

Chlorophyll breakdown in senescent cotyledons of rape, Brassica napus L.: Enzymatic cleavage of phaeophorbide a in vitro

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