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

• 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

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.