Chloroplast biogenesis: Quantitative determination of monovinyl and divinyl chlorophyll(ide) a and b by spectrofluorometry

Wu, Shaowen; Mayasich, Joseph M.; Rebeiz, Constantin A.

doi:10.1016/0003-2697(89)90641-6

Cited by 18 publications

(9 citation statements)

References 19 publications

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“…The reaction was initiated by addition of DV Chlide a, and allowed to proceed for 5 min at 25°C. DV Chlide a was added in 25-30 l of 80% acetone, to a final concentration of 1-2 M. Conversion of DV Chlide a to MV Chlide a was determined by combined room temperature and 77 K spectrofluorometry as described below (6,12).…”

Section: Methodsmentioning

confidence: 99%

Chloroplast Biogenesis 84: Solubilization and Partial Purification of Membrane-Bound [4-Vinyl] Chlorophyllide a Reductase from Etiolated Barley Leaves

Kolossov

Rebeiz

2001

Analytical Biochemistry

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Section: Methodsmentioning

confidence: 99%

Chloroplast Biogenesis 84: Solubilization and Partial Purification of Membrane-Bound [4-Vinyl] Chlorophyllide a Reductase from Etiolated Barley Leaves

Kolossov

Rebeiz

2001

Analytical Biochemistry

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“…Room temperature spectra were recorded in cylindrical microcells 5 mm in diameter, at emission and excitation bandwidths of 4 nm. Low-temperature fluorescence spectra (77 K) were recorded at emission and excitation bandwidths that varied from 0.5 to 4 nm depending on signal intensity (17,18). The photon count was integrated for 0.5 s at each 1 nm increment.…”

Section: Methodsmentioning

confidence: 99%

Chloroplast Biogenesis 87: Evidence of Resonance Excitation Energy Transfer Between Tetrapyrrole Intermediates of the Chlorophyll Biosynthetic Pathway and Chlorophyll a¶†

Kolossov

Kopetz

Rebeiz

2003

Photochem Photobiol

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The thorough understanding of photosynthetic membrane assembly requires a deeper knowledge of the coordination of chlorophyll (Chl) and thylakoid apoprotein biosynthesis. As a working model for future investigations, we have proposed three Chl-thylakoid apoprotein biosynthesis models, namely, a single-branched Chl biosynthetic pathway (SBP) single-location model, an SBP multilocation model and a multibranched Chl biosynthetic pathway (MBP) sublocation model. Rejection or validation of these models can be probed by determination of resonance excitation energy transfer between various tetrapyrrole intermediates of the Chl biosynthetic pathway and various thylakoid Chl-protein complexes. In this study we describe the detection of resonance energy transfer between protoporphyrin IX (Proto), Mg-Proto and its monomethyl ester (Mp(e)) and divinyl and monovinyl protochlorophyllide a (Pchlide a) and several Chl-protein complexes. Induction of various amounts of tetrapyrrole accumulation in green photoperiodically grown cucumber cotyledons and barley leaves was achieved by dark incubation of excised tissues with delta-aminolevulinic acid (ALA) and various concentrations of 2,2'-dipyridyl for various periods of time. Controls were incubated in distilled water. After plastid isolation, treated and control plastids were diluted in buffered glycerol to the same Chl concentration. Excitation spectra were then recorded at 77 K at emission maxima of about 686, 694 and 738 nm. Resonance excitation energy transfer from Proto, Mp(e) and Pchlide a to Chl-protein complexes emitting at 686, 694 and 738 nm was observed by calculation of treated minus control difference excitation spectra. The occurrence of resonance excitation energy transfer between anabolic tetrapyrroles and Chl-protein complexes appeared as well-defined excitation bands with excitation maxima corresponding to those of Proto, Mp(e) and Pchlide a. Furthermore, it appeared that resonance excitation energy transfer from multiple short-wavelength, medium-wavelength and long-wavelength Proto, Mp(e) and Chlide a sites to various Chl-protein complexes took place. Because resonance excitation transfer from donors to acceptors cannot take place at distances larger than 100 A, it is proposed that the observed resonance excitation energy transfers are not compatible with the SBP single-location Chl biosynthesis thylakoid membrane biogenesis model. The latter assumes that a single-branched Chl biosynthetic pathway located in the center of a 450 x 130 A photosynthetic unit generates all of the Chl needed for the assembly of all Chl-protein complexes.

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“…The former include superoxide dismutase, catalase, and glutathione peroxidase. The latter are to be 2-MV Pchl(ide) b (E463 F643) provided with the diet and include, but are not limited Å 1.04 (E463 F643) 0 0.54 (E440 F635) [4] to, antioxidant vitamins, e.g., tocopherols, carotenoids, and ascorbate. Furthermore, evidence accumulates of a 2-MV Pchl(ide) a (E440 F635) protective role of other microcomponents of the diet dur-Å 1.04 (E440 F635) 0 0.08 (E463 F643).…”

mentioning

confidence: 99%

Quantitative Determination of 2-Monovinyl Protochlorophyll(ide)bby Spectrofluorometry

Ioannides

Shedbalkar

Rebeiz

1997

Analytical Biochemistry

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Chloroplast biogenesis: Quantitative determination of monovinyl and divinyl chlorophyll(ide) a and b by spectrofluorometry

Cited by 18 publications

References 19 publications

Chloroplast Biogenesis 84: Solubilization and Partial Purification of Membrane-Bound [4-Vinyl] Chlorophyllide a Reductase from Etiolated Barley Leaves

Chloroplast Biogenesis 84: Solubilization and Partial Purification of Membrane-Bound [4-Vinyl] Chlorophyllide a Reductase from Etiolated Barley Leaves

Chloroplast Biogenesis 87: Evidence of Resonance Excitation Energy Transfer Between Tetrapyrrole Intermediates of the Chlorophyll Biosynthetic Pathway and Chlorophyll a¶†

Quantitative Determination of 2-Monovinyl Protochlorophyll(ide)bby Spectrofluorometry

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