Effect of the electron density of the heme Fe Atom on the Fe-histidine coordination bond in deoxy myoglobin

Ryu Nishimura, Tomokazu Shibata, Hulin Tai, Izumi Ishigami, Sachiko Yanagisawa, Takashi Ogura, Saburo Neya, Akihiro Suzuki, Yasuhiko Yamamoto

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The stretching frequency of the coordination bond between the heme Fe atom and proximal histidine (His93) Nεatom (νFe-His), and the NMR shift of the His93NδH proton (His93NδH shift) of the deoxy form of a hemoprotein have been used to determine the electronic nature of the His93 imidazole highly relevant to regulation of heme Fe reactivity. We determined the νFe-Hisvalues and His93NδH shifts of the deoxy forms of myoglobins reconstituted with artificial heme cofactors possessing strongly electron-withdrawing trifluoromethyl (CF3) group(s) as peripheral side chain(s). The study revealed that the bond between the heme Fe and His93 becomes stronger with increasing number of CF3substitutions due to an increase in acidity of the His93NδH hydrogen bonded to the carbonyl O atom of Leu89. Thus, the present study demonstrated that the electronic nature of the His93 imidazole in deoxy Mb is affected by electronic perturbation induced by chemical modification of the heme cofactor.

Original languageEnglish (US)
Pages (from-to)905-911
Number of pages7
JournalBulletin of the Chemical Society of Japan
Volume87
Issue number8
DOIs
StatePublished - Jan 1 2014

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Myoglobin
Heme
Histidine
Carrier concentration
Atoms
Chemical modification
Acidity
Stretching
Protons
Hydrogen
Nuclear magnetic resonance
Electrons
imidazole

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Effect of the electron density of the heme Fe Atom on the Fe-histidine coordination bond in deoxy myoglobin. / Nishimura, Ryu; Shibata, Tomokazu; Tai, Hulin; Ishigami, Izumi; Yanagisawa, Sachiko; Ogura, Takashi; Neya, Saburo; Suzuki, Akihiro; Yamamoto, Yasuhiko.

In: Bulletin of the Chemical Society of Japan, Vol. 87, No. 8, 01.01.2014, p. 905-911.

Research output: Contribution to journalArticle

Nishimura, R, Shibata, T, Tai, H, Ishigami, I, Yanagisawa, S, Ogura, T, Neya, S, Suzuki, A & Yamamoto, Y 2014, 'Effect of the electron density of the heme Fe Atom on the Fe-histidine coordination bond in deoxy myoglobin', Bulletin of the Chemical Society of Japan, vol. 87, no. 8, pp. 905-911. https://doi.org/10.1246/bcsj.20130331
Nishimura, Ryu ; Shibata, Tomokazu ; Tai, Hulin ; Ishigami, Izumi ; Yanagisawa, Sachiko ; Ogura, Takashi ; Neya, Saburo ; Suzuki, Akihiro ; Yamamoto, Yasuhiko. / Effect of the electron density of the heme Fe Atom on the Fe-histidine coordination bond in deoxy myoglobin. In: Bulletin of the Chemical Society of Japan. 2014 ; Vol. 87, No. 8. pp. 905-911.
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abstract = "The stretching frequency of the coordination bond between the heme Fe atom and proximal histidine (His93) Nεatom (νFe-His), and the NMR shift of the His93NδH proton (His93NδH shift) of the deoxy form of a hemoprotein have been used to determine the electronic nature of the His93 imidazole highly relevant to regulation of heme Fe reactivity. We determined the νFe-Hisvalues and His93NδH shifts of the deoxy forms of myoglobins reconstituted with artificial heme cofactors possessing strongly electron-withdrawing trifluoromethyl (CF3) group(s) as peripheral side chain(s). The study revealed that the bond between the heme Fe and His93 becomes stronger with increasing number of CF3substitutions due to an increase in acidity of the His93NδH hydrogen bonded to the carbonyl O atom of Leu89. Thus, the present study demonstrated that the electronic nature of the His93 imidazole in deoxy Mb is affected by electronic perturbation induced by chemical modification of the heme cofactor.",
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AU - Tai, Hulin

AU - Ishigami, Izumi

AU - Yanagisawa, Sachiko

AU - Ogura, Takashi

AU - Neya, Saburo

AU - Suzuki, Akihiro

AU - Yamamoto, Yasuhiko

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AB - The stretching frequency of the coordination bond between the heme Fe atom and proximal histidine (His93) Nεatom (νFe-His), and the NMR shift of the His93NδH proton (His93NδH shift) of the deoxy form of a hemoprotein have been used to determine the electronic nature of the His93 imidazole highly relevant to regulation of heme Fe reactivity. We determined the νFe-Hisvalues and His93NδH shifts of the deoxy forms of myoglobins reconstituted with artificial heme cofactors possessing strongly electron-withdrawing trifluoromethyl (CF3) group(s) as peripheral side chain(s). The study revealed that the bond between the heme Fe and His93 becomes stronger with increasing number of CF3substitutions due to an increase in acidity of the His93NδH hydrogen bonded to the carbonyl O atom of Leu89. Thus, the present study demonstrated that the electronic nature of the His93 imidazole in deoxy Mb is affected by electronic perturbation induced by chemical modification of the heme cofactor.

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