Chemical properties of sperm whale myoglobins reconstituted with monopropionate hemins

Takashi Hayashi; Tomoyuki Nakagawa; Katsuyoshi Harada; Takashi Matsuo; Yutaka Hitomi; Yoshio Hisaeda

doi:10.1246/cl.2004.1512

Chemical properties of sperm whale myoglobins reconstituted with monopropionate hemins

Takashi Hayashi, Tomoyuki Nakagawa, Katsuyoshi Harada, Takashi Matsuo, Yutaka Hitomi, Yoshio Hisaeda

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1512-1513
Number of pages	2
Journal	Chemistry Letters
Volume	33
Issue number	11
DOIs	https://doi.org/10.1246/cl.2004.1512
Publication status	Published - Nov 5 2004

All Science Journal Classification (ASJC) codes

Chemistry(all)

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10.1246/cl.2004.1512

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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.",

author = "Takashi Hayashi and Tomoyuki Nakagawa and Katsuyoshi Harada and Takashi Matsuo and Yutaka Hitomi and Yoshio Hisaeda",

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AU - Hayashi, Takashi

AU - Nakagawa, Tomoyuki

AU - Harada, Katsuyoshi

AU - Matsuo, Takashi

AU - Hitomi, Yutaka

AU - Hisaeda, Yoshio

PY - 2004/11/5

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N2 - 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.

AB - 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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JO - Chemistry Letters

JF - Chemistry Letters

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ER -

Chemical properties of sperm whale myoglobins reconstituted with monopropionate hemins

Abstract

All Science Journal Classification (ASJC) codes

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