TEMPERATURE DEPENDENCE OF PHOSPHORESCENCE PARAMETERS OF PHYLOGENETICALLY DISTANT APOMYOGLOBINS

Abstract. The triplet state lifetime and the position of the O—O vibrational band of the tryptophanyl phosphorescence spectrum of two philogenetically distant apomyoglobins, i.e. tuna and sperm whale apomyoglobin, have been studied at different temperatures. The temperature dependence of the two pho...

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Bibliographic Details
Published in:Photochemistry and Photobiology
Main Authors: Bismuto, Ettore, Strambini, Giovanni B., IRACE, GAETANO
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 1987
Subjects:
Physical and Theoretical Chemistry
General Medicine
Biochemistry
Sperm whale
Online Access:http://dx.doi.org/10.1111/j.1751-1097.1987.tb07875.x
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1751-1097.1987.tb07875.x
https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1751-1097.1987.tb07875.x
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Summary:Abstract. The triplet state lifetime and the position of the O—O vibrational band of the tryptophanyl phosphorescence spectrum of two philogenetically distant apomyoglobins, i.e. tuna and sperm whale apomyoglobin, have been studied at different temperatures. The temperature dependence of the two phosphorescence parameters revealed that the tryptophanyl microenvironment possesses different dynamic characteristics in the two examined proteins. In particular, the tryptophanyl side chain of tuna apomyoglobin was found embedded into a less rigid microenvironmental cluster which possesses a higher degree of internal flexibility than that of sperm whale apomyoglobin.

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