Protochlorophyllide transformations and chlorophyll accumulation in epicotyls of pea (<i>Pisum sativum</i>)

Böddi, Béla; Evertsson, Ivar; Ryberg, Margareta; Sundqvist, Christer

doi:10.1111/j.1399-3054.1996.tb00246.x

Cited by 31 publications

(2 citation statements)

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“…The long-wavelength form of Pchlide has in general a fluorescence peak around 657 nm, but in the Alaska pea, as in many other pea cultivars, this peak is slightly blue-shifted to 654 nm (cf. Bö ddi et al 1996). This spectral difference can reflect a structural difference in the NADPH-Pchlide-POR complex.…”

Section: Discussionmentioning

confidence: 99%

Protochlorophyllide, NADPH‐protochlorophyllide oxidoreductase, and chlorophyll formation in the lip1 mutant of pea

Seyyedi

Timko

Sundqvist

1999

Physiologia Plantarum

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The early steps in chloroplast development were characterized in wild‐type pea (Pisum sativum L. cv. Alaska) and the lip1 mutant with light‐independent photomorphogenesis. When grown in darkness, the wild type had a long slender epicotyl and undeveloped leaves while the lip1 mutant had seedlings with short epicotyls and well‐developed leaves. The leaves of the wild‐type Alaska pea had two fluorescence emission maxima of protochlorophyllide (Pchlide) at 630 and 655 nm. Leaves from the lip1 mutant had a fluorescence emission maximum at 632 nm with only a small shoulder at 655 nm. Flash irradiation of wild‐type leaves gave chlorophyllide (Chlide) with a fluorescence peak at 692 nm exhibiting a Shibata shift to 682 nm. The Chlide formed in lip1 leaves was diminutive with a maximum at 677 nm. Continuous irradiation led to the formation of a significant amount of Chlide, the esterification of which was considerably delayed in the lip1 plants. The transcript level of NADPH‐protochlorophyllide oxidoreductase (POR) was the same in dark‐grown lip1 and wild‐type leaves. Sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) and immunoblots indicated the presence of POR (EC 1.3.1.33) in leaves of both wild‐type and lip1 dark‐grown seedlings. Just one band at 36 kDa was detectable. The level of the protein both in wild type and the lip1 mutant was stable during 6 h of irradiation. Large regular prolamellar bodies (PLBs) were common in dark‐grown wild‐type etioplasts, whereas lip1 etioplast inner membranes consisted mostly of prothylakoids (PTs). When present in lip1, the PLBs were rudimentary, but often a number of plastoglobuli were assembled in the etioplasts. The high content of POR was unexpected considering the observed lack of PLBs and Pchlide fluorescing at 655 nm. Immunogold labeling showed a distribution of POR among the PTs. It can be concluded that the formation and accumulation of POR in pea is, in itself, insufficient to induce PLB formation or the formation of long‐wavelength Pchlide forms. It appears that there also must be other factor(s) of importance, which are significant for the formation of the PLBs.

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Section: Discussionmentioning

confidence: 99%

Protochlorophyllide, NADPH‐protochlorophyllide oxidoreductase, and chlorophyll formation in the lip1 mutant of pea

Seyyedi

Timko

Sundqvist

1999

Physiologia Plantarum

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“…One of them is specific for etiolated plants and is related to the presence of a prolamellar body, the other one is found both in etiolated plants and in lightadapted plants in the (pro)thylakoid fraction (Franck et al 1993;Durchan & Lebedev 1995;Lebedev et al 1995;Böddi et al 1996). In etiolated seedlings two forms of LPOR, POR-A and POR-B are expressed.…”

Section: Light-dependent Protochlorophyllide Oxidoreductasementioning

confidence: 99%

A short overview of chlorophyll biosynthesis in algae

et al. 2008

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Chlorophylls are the most abundant classes of natural pigments and their biosynthesis is therefore a major metabolic activity in the ecosphere. Two pathways exist for chlorophyll biosynthesis, one taking place in darkness and the other requiring continuous light as a precondition. The key process for Chl synthesis is the reduction of protochlorophyllide (Pchlide). This enzymatic reaction is catalysed by two different enzymes -DPOR (dark-operative Pchlide oxidoreductase) or the structurally distinct LPOR (light-dependent Pchlide oxidoreductase). DPOR which consists of three subunits encoded by three plastid genes in eukaryotes was subject of our study. A short overview of our present knowledge of chlorophyll biosynthesis in Chlamydomonas reinhardtii in comparison with other plants is presented.

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