The molecular basis of the coloration mechanism in lobster shell: β-Crustacyanin at 3.2-Å resolution

  title={The molecular basis of the coloration mechanism in lobster shell: $\beta$-Crustacyanin at 3.2-Å resolution},
  author={M. Cianci and P. Rizkallah and A. Olczak and J. Raftery and N. Chayen and P. F. Zagalsky and J. Helliwell},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  pages={9795 - 9800}
The binding of the carotenoid astaxanthin (AXT) in the protein multimacromolecular complex crustacyanin (CR) is responsible for the blue coloration of lobster shell. The structural basis of the bathochromic shift mechanism has long been elusive. A change in color occurs from the orange red of the unbound dilute AXT (λmax 472 nm in hexane), the well-known color of cooked lobster, to slate blue in the protein-bound live lobster state (λmax 632 nm in CR). Intriguingly, extracted CR becomes red on… Expand
On the origin and variation of colors in lobster carapace.
It is found that enolate formation is possible within the protein environment and associated with a large bathochromic shift, thus offering a cogent explanation for the blue-black color and the response to thermal denaturation and revealing the chemistry of astaxanthin upon complex formation. Expand
Origin of the bathochromic shift of astaxanthin in lobster protein: 2D electronic spectroscopy investigation of β-crustacyanin.
The origin of the shift is proposed to be caused by two major effects: conformational changes of astaxanthin molecules (increase in effective conjugation length) together with increased charge-transfer character of the S2 state, and put the bathochromic shift in the broad perspective of other "blue" carotenoids properties. Expand
Unravelling the chemical basis of the bathochromic shift in the lobster carapace; new crystal structures of unbound astaxanthin, canthaxanthin and zeaxanthin.
These six crystal structures provide an ensemble of experimentally derived results that allow several key parameters, thought to influence colour tuning of the bathochromic shift of astaxanthin in crustacyanin, to be varied. Expand
Protein-bound chromophores astaxanthin and phytochromobilin: excited state quantum chemical studies.
The application of time-dependent density functional theory and other single-reference quantum chemical excited state methods have contributed to shed new light on the origin of the >0.5 eV bathochromic shift of the electronic absorption by the carotenoid astaxanthin in the protein macromolecular complex crustacyanin. Expand
Circular dichroism and absorption spectroscopic data reveal binding of the natural cis-carotenoid bixin to human α1-acid glycoprotein
Using circular dichroism (CD) and electronic absorption spectroscopy techniques, interaction of the natural dietary cis-carotenoid bixin with an important human plasma protein in vitro wasExpand
Evolution of a novel carotenoid-binding protein responsible for crustacean shell color.
It is submitted that the origin of the CRCN gene family early in the evolution of malacostracan crustaceans significantly contributed to the success of this group of arthropods. Expand
Characterisation of the carotenoprotein found in carapace shells of Jasus lalandii.
  • E. Timme, D. Walwyn, A. Bailey
  • Biology, Medicine
  • Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
  • 2009
Carotenoprotein, containing astaxanthin as the prosthetic group was extracted from the carapace shells of the lobster, Jasus lalandii, showing potential for its use as a natural water soluble food colourant or temperature sensitive indicator. Expand
Photophysics of deinoxanthin, the keto-carotenoid bound to the main S-layer unit of Deinococcus radiodurans.
  • F. Adamec, Domenica Farci, +5 authors T. Polívka
  • Medicine, Chemistry
  • Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2020
The keto-carotenoid deinoxanthin, which occurs in the UV-resistant bacterium Deinococcus radiodurans, has been investigated by ultrafast time-resolved spectroscopy techniques and the results suggest a rather loosely bound carotenoids in SDBC, making it very distinct from other carOTenoid-binding proteins such as Orange Carotenoidal Protein (OCP) or crustacyanin. Expand
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP
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A comparative study of three signaling forms of the orange carotenoid protein
The data support the idea that the red form of OCP is a molten globule-like protein in which interactions between the carotenoid and the C-terminal domain are preserved, and are corroborated by hydrodynamic analysis of proteins by dynamic light scattering and analytical size-exclusion chromatography. Expand


A study of protein-carotenoid interactions in the astaxanthin-protein crustacyanin by absorption and Stark spectroscopy; evidence for the presence of three spectrally distinct species.
Molecular mechanisms underlying the peculiar spectral properties of the carotenoid astaxanthin in alpha-crustacyanin, the blue carotenoprotein isolated from the exoskeleton of the lobster HomarusExpand
Mechanisms of spectral shifts in lobster carotenoproteins. The resonance Raman spectra of ovoverdin and the crustacyanins.
Resonance Raman data have been used to elucidate the mechanisms of the absorption spectral shifts occurring for astaxanthin upon binding to the carotenoproteins, ovoverdin and alpha-,beta- andExpand
Structure of lobster apocrustacyanin A1 using softer X-rays.
This paper describes the structure solution of CRTC in the form of the A(1) dimer based on use of softer X-rays, which can now be used as a search motif in the structural studies of the oligomeric forms alpha- and beta-crustacyanins, which contain bound astaxanthin molecules. Expand
The mechanism of the colour shift of astaxanthin in α-crustacyanin as investigated by 13C MAS NMR and specific isotope enrichment
By selective isotope enrichment of astaxanthin, MAS NMR and semi-empirical modelling, ligand-protein interactions associated with the red shift in a-crustacyanin, the major blue astaxanthin bindingExpand
Complete sequence and model for the C1 subunit of the carotenoprotein, crustacyanin, and model for the dimer, beta-crustacyanin, formed from the C1 and A2 subunits with astaxanthin.
The complete sequence has been determined for the C1 subunit of crustacyanin, an astaxanthin-binding protein from the carapace of the lobster Homarus gammarus, and a tentative model for the dimer, beta-crustacyanIn, formed between the two subunits with their associated carotenoid ligands, is discussed. Expand
Studies on the quaternary structure of the lobster exoskeleton carotenoprotein, crustacyanin.
Although each apoprotein has the ability to form the dimer, β-crustacyanin, on combination with astaxanthin, association between pairs of apoproteins, one from each set, occurs more readily. Expand
Crystal Structure of Sensory Rhodopsin II at 2.4 Angstroms: Insights into Color Tuning and Transducer Interaction
We report an atomic-resolution structure for a sensory member of the microbial rhodopsin family, the phototaxis receptor sensory rhodopsin II (NpSRII), which mediates blue-light avoidance by theExpand
Crystallization and initial X-ray analysis of beta-crustacyanin, the dimer of apoproteins A2 and C1, each with a bound astaxanthin molecule.
Crystals of beta-crustacyanin, a carotenoid-binding protein from lobster carapace, have been grown under oil from solutions containing sodium potassium phosphate as precipitant but are very radiation sensitive, limiting the resolution of usable data. Expand
Crystallization, crystal structure analysis and preliminary molecular model of the bilin binding protein from the insect Pieris brassicae.
The bilin binding protein of the butterfly Pieris brassicae has been prepared, crystallized and its crystal structure determined at high resolution using film and FAST area detector intensity data.Expand
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Interestingly the overall three‐dimensional fold of the insecticyanin subunit shows remarkable similarity to the structural motifs of bovine beta‐lactoglobulin and the human serum retinol‐binding protein. Expand