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

@article{Cianci2002TheMB,
  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},
  year={2002},
  volume={99},
  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
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