Chemical Properties of Sperm Whale Myoglobins Reconstituted with Monopropionate Hemins

Abstract The binding behavior of two heme-propionate side chains in sperm whale myoglobin was evaluated using artificially created hemins, 6-methyl-7-propionate- and 6-propionate-7-methyl-protohemin IX. From the thermodynamic study of the hemin binding to apomyoglobin, it was found that two heme-pro...

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Bibliographic Details
Published in:Chemistry Letters
Main Authors: Hayashi, Takashi, Nakagawa, Tomoyuki, Harada, Katsuyoshi, Matsuo, Takashi, Hitomi, Yutaka, Hisaeda, Yoshio
Format: Article in Journal/Newspaper
Language:English
Published: Oxford University Press (OUP) 2004
Subjects:
Sperm whale
Online Access:http://dx.doi.org/10.1246/cl.2004.1512
https://academic.oup.com/chemlett/article-pdf/33/11/1512/55583646/cl.2004.1512.pdf
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Summary:Abstract The binding behavior of two heme-propionate side chains in sperm whale myoglobin was evaluated using artificially created hemins, 6-methyl-7-propionate- and 6-propionate-7-methyl-protohemin IX. From the thermodynamic study of the hemin binding to apomyoglobin, it was found that two heme-propionates clearly contribute to the stabilization of the hemin in the protein matrix.

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