Studies on Plant Bile Pigments, II. Chemical and Photochemical Oxygenation of a Phytochrome P<sub><b>r</b></sub>Chromophore Model Pigment to Purpurins

Scheer, Hugo; Linsenmeier, U.; Krauss, Corinna

doi:10.1515/bchm2.1977.358.1.185

Cited by 28 publications

(3 citation statements)

References 16 publications

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“…Formation of bile pigment metal complexes (e.g., with Zn2+) in methanol is favored kinetically, as compared to complex formation by the macrocyclic porphyrins, but is not favored thermodynamically (cf. ref 46). For metal ions such as Cu2+ which bind readily and strongly to the central four-nitrogen site, no peripheral complexes have been observed, but central complexes form directly.…”

Section: Discussionmentioning

confidence: 99%

Peripheral metal complexes: chlorophyll "isomers" with magnesium bound to the ring E .beta.-keto ester system

Scheer¹,

Katz²

1978

J. Am. Chem. Soc.

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Section: Discussionmentioning

confidence: 99%

Peripheral metal complexes: chlorophyll "isomers" with magnesium bound to the ring E .beta.-keto ester system

Scheer¹,

Katz²

1978

J. Am. Chem. Soc.

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“…1). As the bilins become more liable to oxidation at higher pH [26], a pH ≤ 7.5 was favoured, and usually buffers of pH 7.5 were used in this work.…”

Section: Other Factors Influencing Activitymentioning

confidence: 99%

Characterization of phycoviolobilin phycoerythrocyanin‐α84‐cystein‐lyase‐(isomerizing) from Mastigocladus laminosus

Zhao

Wang

et al. 2002

European Journal of Biochemistry

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Cofactor requirements and enzyme kinetics have been studied of the novel, dual-action enzyme, the isomerizing phycoviolobilinphycoerythrocyanin-a84-cystein-lyase(PVB-PEC-lyase) from Mastigocladus laminosus, which catalyses both the covalent attachment of phycocyanobilin to PecA, the apo-a-subunit of phycoerythrocyanin, and its isomerization to phycoviolobilin. Thiols and the divalent metals, Mg 2+ or Mn 2+ , were required, and the reaction was aided by the detergent, Triton X-100. Phosphate buffer inhibits precipitation of the proteins present in the reconstitution mixture, but at the same time binds the required metal. Kinetic constants were obtained for both substrates, the chromophore (K m ¼ 12-16 lM, depending on [PecA], k cat 1.2 · 10 )4 AEs )1 ) and the apoprotein (K m ¼ 2.4 lM at 14 lM PCB, k cat ¼ 0.8 · 10 )4 AEs )1 ). The kinetic analysis indicated that the reconstitution reaction proceeds by a sequential mechanism. By a combination of untagged and His-tagged subunits, evidence was obtained for a complex formation between PecE and PecF (subunits of PVB-PEClyase), and by experiments with single subunits for the prevalent function of PecE in binding and PecF in isomerizing the chromophore.

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“…Under mildly basic con ditions the zinc complex of A-dihydrobilindione 1 loses the hydrogenated ring A to form 2 [6] . The biliprotein phycocyanin 3 is cleaved in an analogous manner.…”

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Two Mild, Regioselective Methods of Degrading Biliprotein Chromophores

Kufer¹,

Krauss²,

Scheer³

1982

Angew. Chem. Int. Ed. Engl.

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Biliproteins-receptor proteins in photosynthesis and photomorphogenesis-consist of bile pigments, which are covalently bound via a thioether bond at ring A to a protein; a second bond is disputed (see Discussion in [2J ). We describe here two mild degradation procedures for free and protein-bound bile pigments. These methods, unlike chromic acid degradation 151 , result in the retention of substantial information on the substituents at the a-pyrrolic and methine positions.

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Studies on Plant Bile Pigments, II. Chemical and Photochemical Oxygenation of a Phytochrome P_rChromophore Model Pigment to Purpurins

Cited by 28 publications

References 16 publications

Peripheral metal complexes: chlorophyll "isomers" with magnesium bound to the ring E .beta.-keto ester system

Peripheral metal complexes: chlorophyll "isomers" with magnesium bound to the ring E .beta.-keto ester system

Characterization of phycoviolobilin phycoerythrocyanin‐α84‐cystein‐lyase‐(isomerizing) from Mastigocladus laminosus

Two Mild, Regioselective Methods of Degrading Biliprotein Chromophores

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Studies on Plant Bile Pigments, II. Chemical and Photochemical Oxygenation of a Phytochrome PrChromophore Model Pigment to Purpurins

Cited by 28 publications

References 16 publications

Peripheral metal complexes: chlorophyll "isomers" with magnesium bound to the ring E .beta.-keto ester system

Peripheral metal complexes: chlorophyll "isomers" with magnesium bound to the ring E .beta.-keto ester system

Characterization of phycoviolobilin phycoerythrocyanin‐α84‐cystein‐lyase‐(isomerizing) from Mastigocladus laminosus

Two Mild, Regioselective Methods of Degrading Biliprotein Chromophores

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Studies on Plant Bile Pigments, II. Chemical and Photochemical Oxygenation of a Phytochrome P_rChromophore Model Pigment to Purpurins