Phytochrome models. 6. Conformation control by membrane of biliverdin dimethyl ester incorporated into lipid vesicles

Tegmo-Larsson, Inga Mai; Braslavsky, Silvia E.; Culshaw, Stephen; Ellul, Raymond; Nicolau, Claude; Schaffner, Kurt

doi:10.1021/ja00414a019

Cited by 24 publications

(6 citation statements)

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“…Similar conformational changes have been reported upon protonation of the nitrogen of pyrrole ring B generating the cationic state (Structure 1.H + in Fig. 2) (20–23). Under these conditions, the internal hydrogen‐bonding network breaks down and stretched conformations of the macrocycle may occur.…”

Section: Introductionsupporting

confidence: 78%

“…In addition, small populations of partially extended ZZZass and ZZZsas conformers may co‐exist in a dynamic equilibrium with the ZZZsss geometry (18,19). Protic and amphiphilic solvents may further disturb this structure and lead to more stretched conformations (20–23). The generation of extended configurations upon protonation was suggested already very early in bilin spectroscopy (24).…”

Section: Introductionmentioning

confidence: 99%

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Role of the Protein Cavity in Phytochrome Chromoprotein Assembly and Double‐bond Isomerization: A Comparison with Model Compounds

Rohmer

Lang

Gärtner

et al. 2010

Photochem & Photobiology

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Difference patterns of (13)C NMR chemicals shifts for the protonation of a free model compound in organic solution, as reported in the literature (M. Stanek, K. Grubmayr [1998] Chem. Eur. J.4, 1653-1659), were compared with changes in the protonation state occurring during holophytochrome assembly from phycocyanobilin (PCB) and the apoprotein. Both processes induce identical changes in the NMR signals, indicating that the assembly process is linked to protonation of the chromophore, yielding a cationic cofactor in a heterogeneous, quasi-liquid protein environment. The identity of both difference patterns implies that the protonation of a model compound in solution causes a partial stretching of the geometry of the macrocycle as found in the protein. In fact, the similarity of the difference pattern within the bilin family for identical chemical transformations represents a basis for future theoretical analysis. On the other hand, the change of the (13)C NMR chemical shift pattern upon the Pr --> Pfr photoisomerization is very different to that of the free model compound upon ZZZ --> ZZE photoisomerization. Hence, the character of the double-bond isomerization in phytochrome is essentially different from that of a classical photoinduced double-bond isomerization, emphasizing the role of the protein environment in the modulation of this light-induced process.

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Section: Introductionsupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Role of the Protein Cavity in Phytochrome Chromoprotein Assembly and Double‐bond Isomerization: A Comparison with Model Compounds

Rohmer

Lang

Gärtner

et al. 2010

Photochem & Photobiology

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“…Possibly, Triton X‐100 modifies the conformation of chromophore, to a form suitable for the PVB‐PEC‐lyase to act on, and unfavourable for PecA to bind spontaneously to PCB. Changes of the conformational equilibria of bile pigments have been reported in a variety of environments [27,28], including lipids [29]. It is possible that, by analogy, PecE/F also changes the conformation of the bilin in the course of the addition reaction (see below).…”

mentioning

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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“…This compound is frequently used as a standard in the red, where many biological chromophores display emission (e.g. biliverdin dimethyl ester, Tegmo-Larsson et al, 1981, andphytochrome, Wendler et al, 1984).…”

Section: Modulated Excitationmentioning

confidence: 99%

“…Therefore, the lifetime of the energy storing species can be deduced in principle from a knowledge of 7,. LIOAS permitted also the detection of the photoisomerization of BVE embedded in lipid vesicles (Tegmo-Larsson et al, 1981). This technique is well suited for the study of nonradiative processes in scattering samples.…”

Section: Pulsed Excitationmentioning

confidence: 99%

Photo Acoustic and Photothermal Methods Applied to the Study of Radiationless Deactivation Processes in Biological Systems and in Substances of Biological Interest

Phytochrome models. 6. Conformation control by membrane of biliverdin dimethyl ester incorporated into lipid vesicles

Cited by 24 publications

References 0 publications

Role of the Protein Cavity in Phytochrome Chromoprotein Assembly and Double‐bond Isomerization: A Comparison with Model Compounds

Role of the Protein Cavity in Phytochrome Chromoprotein Assembly and Double‐bond Isomerization: A Comparison with Model Compounds

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

Photo Acoustic and Photothermal Methods Applied to the Study of Radiationless Deactivation Processes in Biological Systems and in Substances of Biological Interest

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