Spectroscopic properties of protochlorophyll forms in Triton X-100 detergent micelles

Böddi, Béla; Kovács, K.; Láng, F.

doi:10.1016/0005-2728(83)90079-8

Cited by 16 publications

(8 citation statements)

References 28 publications

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“…A conformational change of the protein is implied. This conclusion is based on the similarity of the CD and electronic spectra of protochlorophyll in detergent micelles to these kind of spectra of Pchlide in PLBs (Boddi et al 1983(Boddi et al , 1990). An earlier view attributed the Shibata shift to the change in environment of the Chlide caused by its displacement from the complex by incoming Pchlide.…”

Section: Discussionmentioning

confidence: 98%

Isoelectric focusing of pigment‐protein complexes solubilized from non‐irradiated and irradiated prolamellar bodies

Wiktorsson

Ryberg

Gough

et al. 1992

Physiologia Plantarum

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Preparative isoelectric focusing was employed to compare the association of protochlorophyllide and chlorophyllide with the enzyme NADPH‐protochlorophyllide oxidoreductase (PCR; EC 1.3.1.33). Photoactive protochlorophyllide‐PCR complexes were solubilized with 1‐O‐n‐octyl‐β‐d‐glucopyranoside from non‐irradiated prolamellar bodies of wheat (Triticum aestivum). Also, chlorophyllide‐PCR complexes were solubilized from prolamellar bodies irradiated under conditions either preventing or favouring a spectral shift of chlorophyllide to shorter wavelengths. Independently of the treatment prior to the solubilization, the pigments and the PCR focused together at pHs of 4 to 5. The results indicate that protochlorophyllide‐PCR complexes are conformationally similar to chlorophyllide‐PCR complexes. The results support the hypothesis that the spectral shift, referred to as the Shibata shift, reflects a breaking‐up of large chlorophyllide‐PCR aggregates to smaller chlorophyllide‐PCR units, rather than a dissociation of the chlorophyllide from the enzyme protein.

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Section: Discussionmentioning

confidence: 98%

Isoelectric focusing of pigment‐protein complexes solubilized from non‐irradiated and irradiated prolamellar bodies

Wiktorsson

Ryberg

Gough

et al. 1992

Physiologia Plantarum

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“…The shape of the CD spectrum of Pchl in micelles of Triton X-100 strongly depended on the pigment concentration. 19 Even preparations of the enzyme-substrate complex have been described with either a negative CD band at 647 nm and a positive CD band at 637 nm, 20 a positive CD band at 652 nm and a negative CD band at 638 nm, 3 or two negative CD bands at 635 and 615 nm. 21 The CD spectrum of monomeric Pchlide a determined in this paper resembles the CD spectrum of monomeric Pchl a isolated from pumpkin seed coats.…”

Section: Discussionmentioning

confidence: 99%

Absolute Configuration of Protochlorophyllideaand Substrate Specificity of NADPH−Protochlorophyllide Oxidoreductase

et al. 1996

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Protochlorophyllide a was isolated from dark-grown barley (Hordeum Vulgare L.) seedlings. The circular dichroism spectrum was identical with that of protochlorophyll a prepared from chlorophyll a by dehydrogenation. The mirror image was obtained for the circular dichroism spectrum of protochlorophyllide a′ that had been prepared from chlorophyllide a′. These results prove the 13 2 (R) configuration of natural protochlorophyllide a. Incubation of the seedlings with 5-aminolevulinate resulted in accumulation of protochlorophyllide a. This proved to be partially racemized already within the plants. Circular dichroism spectra were also obtained for 13 2 (R)-methoxy and 13 2 -(S)-methoxy derivatives of zinc protopheophorbide a that cannot racemize. Using the increment of the methoxy group by comparison with the respective methoxypyro compound, the circular dichroism spectrum of zinc protopheophorbide a was calculated. Kinetics of racemization indicated a faster reaction for zinc than for magnesium complexes. The enzyme NADPH-protochlorophyllide oxidoreductase solubilized from isolated prolamellar bodies of dark-grown wheat (Triticum aestiVum L.) does not accept protochlorophyllide a′ or any compound with substituents at C-13 2 different from protochlorophyllide a. The substrate specificity is compared with that of chlorophyll synthase.

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“…Improved methods have made possible the isolation of etioplast inner membrane fragments with absorption and fluorescence emission spectra similar to those of intact etiolated leaves (Ryberg and Sundqvist, 1982;Lindsten er al., 1988). The CD spectra of fragments of etioplast inner membranes led us to conclude that the 650 nm absorbing PChlide form in vivo is composed of aggregates of several units (ternary complexes of PChlide, NADPH and protein) of the PChlide-reductase in which similar chromophore-chromophore interactions are present as in artificial 650 nm absorbing aggregates (Boddi et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

“…Circular dichroism (CD) spectroscopy of PChlide and PChl containing artificial systems ( 1975;Boddi et al, 1980Boddi et al, , 1983 indicated that the 650 nm absorbing forms of the pigments are aggregates with different molecular arrangements (Boddi et a/., 1980). The comparison of the in vitro results with similar data of in vivo systems are problematic because the C D signal from intact leaves is weak in relation to the light scattering.…”

Section: Introductionmentioning

confidence: 99%

Phototransformation of Aggregated Forms of Protochlorophyllide in Isolated Etioplast Inner Membranes

Böddi

Lindsten

Ryberg

et al. 1990

Photochem & Photobiology

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Irradiation of an etioplast inner membrane fraction caused the transformation of two photoactive spectroscopically different protochlorophyllide forms into two chlorophyllide forms. A weak light flash, 6% of a saturating Hash, preferentially caused the formation of a short wavelength chlorophyllide form absorbing at 672 nm and emitting at 676 nm. A saturating flash resulted in the formation of the 684 nm absorbing form of chlorophyllide with an emission maximum at 698 nm.The circular dichroism (CD) signals of the newly formed chlorophyllide forms indicated that thcy are pigment aggregates of different sizes. These aggregates are probably connected to protochlorophyllide reductase and NADPH or NADP. In the absence of NADPH a decomposition of the pigment aggregates took place as revealed by a decrease in the CD-signal. A model is suggested which describes the structural changes of the pigment-protein aggregates after irradiation.

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Spectroscopic properties of protochlorophyll forms in Triton X-100 detergent micelles

Cited by 16 publications

References 28 publications

Isoelectric focusing of pigment‐protein complexes solubilized from non‐irradiated and irradiated prolamellar bodies

Isoelectric focusing of pigment‐protein complexes solubilized from non‐irradiated and irradiated prolamellar bodies

Absolute Configuration of Protochlorophyllideaand Substrate Specificity of NADPH−Protochlorophyllide Oxidoreductase

Phototransformation of Aggregated Forms of Protochlorophyllide in Isolated Etioplast Inner Membranes

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