Dynamic aspects of the heme-binding site in phylogenetically distant myoglobins

Dynamic aspects of the heme-binding site of myoglobins derived from two phylogenetically distant species, namely sperm whale and bluefin tuna, have been investigated by studying steady-state and time-resolved emission properties of 2-p-toluidinyl-6-naphthalene sulfonic acid (TNS) apomyoglobin conjug...

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Bibliographic Details
Main Authors: Bismuto, Ettore, Irace, Gaetano, Colonna, Giovanni, Jameson, David M, Gratton, Enrico
Format: Article in Journal/Newspaper
Language:unknown
Published: eScholarship, University of California 1987
Subjects:
Animals
Binding Sites
Heme
Myoglobin
Naphthalenesulfonates
Phylogeny
Protein Conformation
Spectrometry
Fluorescence
Tuna
Whales
Physical Sciences
Biological Sciences
Sperm whale
Online Access:https://escholarship.org/uc/item/2hp0q2xh
Description
Summary:Dynamic aspects of the heme-binding site of myoglobins derived from two phylogenetically distant species, namely sperm whale and bluefin tuna, have been investigated by studying steady-state and time-resolved emission properties of 2-p-toluidinyl-6-naphthalene sulfonic acid (TNS) apomyoglobin conjugates. Multi-frequency phase and modulation fluorometry data indicate that charge movements occur in the fluorophore environment during the excited state lifetime in the sperm whale myoglobin system. In the case of the bluefin tuna myoglobin TNS adduct these movements were not detected, indicating that the relaxation processes differ in the two types of myoglobins.

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