ISSN:
1572-8773
Keywords:
Hemocyanin
;
Helix pomatia
;
Fluorescence
;
Conformational transition
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Summary Oxygenation of native hemocyanins β fromHelix pomatia andPanulirus interruptus under conditions of cooperative binding, causes a change in the dynamic behaviour of the internal structure, leading to increased rotational mobility of a class of tryptophan residues emitting above 450 nm. This is associated with the complete depolarization of the emission on a time scale where the large hemocyanin is practically immobile. This class is thought to be very near the active site since it is strongly affected by the copper atoms. Moreover, fluorescence changes of the class of chromophores emitting above 450 nm is more marked in the molluscanHelix hemocyanin than in the arthropodanPanulirus hemocyanin, suggesting a possible difference in the structure of the active site or in the extent of the allosteric transition between the two species. This class of chromophores may by useful probes to monitor ligand-linked conformational change in hemocyanins.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01179508
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