An Improved Method Fòr Extraction, Partial Purification, Separation and Isolation of Chlorophyll from Spinach Leaves

Iriyama, Keiji; Shiraki, Masaru; Yoshiura, Masahiko

doi:10.1080/01483917908060061

Cited by 54 publications

(14 citation statements)

References 16 publications

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“…Chlorophyll a (Chl) was isolated from Spirulina geitleri [22]. [3‐Acetyl]‐chlorophyll a (acetyl‐Chl) was prepared from bacteriochlorophyll a (BChl) by oxidation with 2,3‐dichloro‐5,6‐dicyano‐benzoquinone [23].…”

Section: Methodsmentioning

confidence: 99%

Modification of pigment composition in the isolated reaction center of photosystem II

Gall¹,

Zehetner²,

Scherz³

et al. 1998

FEBS Letters

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The pigment content of isolated reaction centers of photosystem II was modified using an exchange protocol similar to that used for purple bacterial reaction centers. With this method, which is based on incubation of reaction centers at elevated temperature with an excess of chemically modified pigments, it was possible to incorporate [3-acetyl]-chlorophyll a and [Zn]-chlorophyll a into photosystem II reaction centers. Pigment exchange has been verified by absorption, circular dichroism and fluorescence spectroscopy, and quantitated by HPLC analysis of pigment extracts.z 1998 Federation of European Biochemical Societies.

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Section: Methodsmentioning

confidence: 99%

Modification of pigment composition in the isolated reaction center of photosystem II

Gall¹,

Zehetner²,

Scherz³

et al. 1998

FEBS Letters

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“…Chlorophyll a and b were isolated from spinach [45]. For the synthesis of Zn‐17 3 ‐methylpheophorbide b (Zn‐Me‐Pheid b ) , chlorophyll b was demetallated to pheophytin b with acetic acid [46] and the phytyl ester transesterified by refluxing for 1 h under argon with methanol/5% H 2 SO 4 [47].…”

Section: Methodsmentioning

confidence: 99%

Design, synthesis and properties of synthetic chlorophyll proteins

Rau

Snigula

Struck

et al. 2001

European Journal of Biochemistry

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A chemoselective method is described for coupling chlorophyll derivatives with an aldehyde group to synthetic peptides or proteins modified with an aminoxyacetyl group at the :-amino group of a lysine residue. Three templateassembled antiparallel four-helix bundles were synthesized for the ligation of one or two chlorophylls. This was achieved by coupling unprotected peptides to cysteine residues of a cyclic decapeptide by thioether formation. The amphiphilic helices were designed to form a hydrophobic pocket for the chlorophyll derivatives. Chlorophyll derivatives Zn-methylpheophorbide b and Zn-methyl-pyropheophorbide d were used. The aldehyde group of these chlorophyll derivatives was ligated to the modified lysine group to form an oxime bond. The peptide±chlorophyll conjugates were characterized by electrospray mass spectrometry, analytical HPLC, and UV/visible spectroscopy. Two four-helix bundle chlorophyll conjugates were further characterized by sizeexclusion chromatography, circular dichroism, and resonance Raman spectroscopy.Keywords: synthetic proteins; chlorophylls; protein design.Proteins containing chlorophyll (Chl) and bacteriochlorophyll (BChl) are essential for the biological conversion of solar to chemical energy. They serve two general functions: (a) the absorption of light and energy transfer and (b) lightinduced ionization and stable charge separation. Interactions of the pigments with each other and with the protein, control their relative orientations and adjust their excited state and redox properties over a wide range. It is a challenge to design proteins with these functions for new applications. Several high-resolution structures of chlorophyll proteins are known that could guide such a design, including two water-soluble light-harvesting complexes, the FMO protein [1,2] and the peridinin-Chl a protein (PCP) [3], and several integral membrane proteins, namely the light-harvesting complexes LH2 [4] and LHCII [5], and reaction centers from purple bacteria [6,7] and photosystem I [8,9]. A resolution sufficient to recognize details of cofactor binding is only available for the FMO protein, PCP, LH2, and the bacterial reaction centers. The structures reveal rather complex binding pockets for these pigments, complicated particularly by the large hydrophobic phytyl tail of the chlorophylls whose principles of interaction with the molecular environment are currently only partly understood. The phytyl-tails are structurally well defined and interact with the protein, the carotenoids and the tails of neighboring chlorophylls. Taking the LH2 from Rhodobacter spheroides as an example, a single phenylalanine seems to be essential to lock such a hydrophobic cluster within the protein [10]. Even more complex properties are indicated by reconstitution studies of native or genetically modified LHCII [11±17]. As an example, a single tryptophan seems critical, in vitro, for the stepwise assembly of the protein with all 12 chlorophyll molecules. The crucial role of only a few amino acids (including a Trp) i...

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“…The isotope 57 Fe (98%) was used for the Mössbauer measurements in place of natural iron. Chlorophylls were extracted from spinach using a method from the literature [8]. Pheophytins were prepared from the chlorophylls (100 mg) by addition of 0.1 Μ HCl (5 ml) to the acetone solution (50 ml) of the chlorophylls.…”

Section: Preparation Of Compoundsmentioning

confidence: 99%

Mössbauer Spectroscopic and Magnetic Properties of Iron(II,III) Pyropheophytins

et al. 1990

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The Mössbauer spectra and effective magnetic moments of (pyropheophytin a)iron(III) chloride and (pyropheophytin b) iron(III) chloride have revealed that the central iron(III) ion is in a high-spin state. The temperature-dependent asymmetry of the Mössbauer spectra is interpreted in terms of slow electronic spin relaxation. The Mössbauer parameters of these complexes are similar to those of corresponding iron(III) porphyrins. The central iron(III) ions in iron(III) pyropheophytins are autoreduced to the ferrous low-spin state in the presence of pyridine. The Mössbauer parameters of the bis-pyridine iron(II) adducts are also similar to those of corresponding iron(II) porphyrins.

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An Improved Method Fòr Extraction, Partial Purification, Separation and Isolation of Chlorophyll from Spinach Leaves

Cited by 54 publications

References 16 publications

Modification of pigment composition in the isolated reaction center of photosystem II

Modification of pigment composition in the isolated reaction center of photosystem II

Design, synthesis and properties of synthetic chlorophyll proteins

Mössbauer Spectroscopic and Magnetic Properties of Iron(II,III) Pyropheophytins

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