Effect of the Electron Density of the Heme Fe Atom on the Fe-Histidine Coordination Bond in Deoxy Myoglobin

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概要

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• The stretching frequency of the coordination bond between the heme Fe atom and proximal histidine (His93) Nε atom (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-His values 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 CF3 substitutions 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.

著者

• Yamamoto Yasuhiko

  Department of Chemistry, University of Tsukuba

• TAI Hulin

  Department of Chemistry, University of Tsukuba

• Yamamoto Yasuhiko

  Department Of Biochemistry And Molecular Vascular Biology Kanazawa University Graduate School Of Med

• Neya Saburo

  Department Of Physical Chemistry Faculty Of Pharmaceutical Sciences Chiba University

• Ogura Takashi

  Picobiology Inst., Grad. Sch. Life Sci., Univ. Hyogo

• Tai Hulin

  Department Of Chemistry University Of Tsukuba

• Shibata Tomokazu

  Department Of Chemistry University Of Tsukuba

• Yanagisawa Sachiko

  Picobiology Institute Graduate School Of Life Science University Of Hyogo

• Suzuki Akihiro

  Department Of Anesthesiology And Critical Care Medicine Asahikawa Medical College

• Ishigami Izumi

  Picobiology Institute, Graduate School of Life Science, University of Hyogo

• Nishimura Ryu

  Department of Chemistry, University of Tsukuba

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