Über die Bindungen zwischen Chromophor und Protein in Biliproteiden, II. Nachweis von Cystein als bindende Aminosäure in B‐Phycoerythrin

Köst-Reyes, Eliana; Köst, Hans‐Peter; Rüdiger, Wolfhart

doi:10.1002/jlac.197519750907

Cited by 35 publications

(8 citation statements)

References 6 publications

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“…The chromopeptide material contained about 2mol of cysteic acid/mol of chromophore. One of these cysteine residues is proposed to be linked through its thiol group to the a-carbon atom ofthe C2 side chain ofring A, as previously proposed for phycoerythrobilin and phycocyanobilin (Crespi & Smith, 1970;Byfield & Zuber, 1972;Kost-Reyes et al, 1975;Williams & Glazer, 1978;Bryant et al, 1978;Muckle et al, 1978;Brown et al, 1979;Killilea et al, 1980;Lundell et al, 1984). The second cysteine residue would be involved in the proposed stable thioether linkage to the a-carbon atom of the C2 side chain of ring D, as depicted in Scheme 1.…”

Section: Structure Of Phycourobilinmentioning

confidence: 75%

Structure and apoprotein linkages of phycourobilin

Killilea¹,

O'Carra²

1985

Biochemical Journal

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R-Phycoerythrin contains two covalently bound bilin prosthetic groups, phycoerythrobilin and phycourobilin. The two chromophore types were separated as their peptide-bound derivatives by subjecting tryptic digests of R-phycoerythrin to adsorption chromatography on Sephadex G-25. The structure and apoprotein linkages of the bound phycoerythrobilin were found to be identical with those previously reported for this phycobilin [Killilea, O'Carra & Murphy (1980) Biochem. J. 187, 311-320]. Phycourobilin is a tetrapyrrole, containing no oxo bridges and has the same order of side chains as IX alpha bilins. The chromophore is linked to the peptide through two and possibly three of its pyrrole rings. One linkage possibly consists of an ester bond between the hydroxy group of a serine residue and the propionic acid side chain of one of the inner rings. The second linkage is a labile thioether bond between a cysteine residue and the C2 side chain of pyrrole ring A. The third linkage is a stable thioether bond between a cysteine residue and the alpha-carbon atom of the C2 side chain of pyrrole ring D. Ring D is unsaturated and is attached to ring C through a saturated carbon bridge. Rings B and C have a conjugated system of five bonds, as found in other urobilinoid pigments. Ring A is attached to ring B via a saturated carbon bridge. Both of the alpha-positions of ring A are in the reduced state, but the ring does contain an unsaturated centre (probably a double bond between the beta-carbon and the ring nitrogen atom). The presence of this double bond and its isomerization into the bridge position between rings A and B would explain the extension of the conjugated system of phycourobilin to that of a phycoerythrobilinoid/rhodenoid pigment in acid or alkali.

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Section: Structure Of Phycourobilinmentioning

confidence: 75%

Structure and apoprotein linkages of phycourobilin

Killilea¹,

O'Carra²

1985

Biochemical Journal

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“…The chromophore of all three phycobiliprotein classes have been found to be covalently bound to the apoprotein through ring A and probably also C [43]. Analysis of a chromopeptide, prepared from B-PE, consisted of valine, leucine, cysteine and phycoerythrobilin [44]. The thiol group of cysteine was identified as the binding group with the side chain of ring A.…”

Section: Biosynthesis and Chromophore Attachmentmentioning

confidence: 99%

Recent Contributions in Phycobiliproteins and Phycobilisomes

Gantt

1977

Photochem & Photobiology

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“…[1][2][3][4][5]; for re views see [6][7][8]). Although the chemical nature of the prostetic groups phycocyanobilin (in phyco cyanins) and phycoerythrobilin (in phycoerythrins) as bile pigment is known for many years [9][10][11][12][13][14] their biosynthetic pathway is still not fully under stood [15][16][17][18][19][20][21][22][23][24] or more or less uninvestigated (phycoerythrobilin).…”

Section: Introductionmentioning

confidence: 99%

Biliverdin IX α, Intermediate and End Product of Tetrapyrolle Biosynthesis

Köst¹,

Benedikt²

1982

Zeitschrift Für Naturforschung C

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Cyanidium caldarium, Phycocyanobilin Biosynthesis, Biliverdin IX a, Turdus merula, Egg Shells Dark-grown cells of the unicellular rhodophyte Cyanidium caldarium were incubated with 17 mmol/1 5-aminolevulinic acid in the dark. The excreted pigments were extracted with chloroform and butanol. The presence of biliverdin IX a in the chloroform-extract (besides phycocyanobilin and other pigments) was demonstrated using TLC, HPLC and chromic acid degradation. A pathway leading to phycocyanobilin is discussed. A green pigment from egg shells of Turdus merula (black bird) was also identified as biliverdin IX a with small amounts of protoporphyrin IX, using the same methods as above.

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Über die Bindungen zwischen Chromophor und Protein in Biliproteiden, II. Nachweis von Cystein als bindende Aminosäure in B‐Phycoerythrin

Cited by 35 publications

References 6 publications

Structure and apoprotein linkages of phycourobilin

Structure and apoprotein linkages of phycourobilin

Recent Contributions in Phycobiliproteins and Phycobilisomes

Biliverdin IX α, Intermediate and End Product of Tetrapyrolle Biosynthesis

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