Characterization of Heme-Coordinating Histidyl Residues of an Engineered Six-Coordinated Myoglobin Mutant Based on the Reactivity with Diethylpyrocarbonate, Mass Spectrometry, and Electron Paramagnetic Resonance Spectroscopy(ENZYMOLOGY, PROTEIN ENGINEERIN

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概要

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• A genetically engineered porcine myoglobin triple mutant(H64V/V68H/H93A)(VHA-Mb) contains 6 non-axial His residues(His24, His36, His48, His81 His82, and His119) besides two candidate axial His residues(His68 and His97). Although previous resonance Raman study on the ferric VHA-Mb were not conclusive for its coordination structure, present EPR parameters of the ferric VHA-Mb were consistent with bis-imidazole coordination of His68/His97. We further investigated the reactivity of these possible His ligands with diethylpyrocarbonate(DEPC) to clarify the coordination structure and their protonation states in ferric form. We found that the non-axial His residues were easily modified with a low concentration of DEPC based on UV spectral changes and MALDI-TOF-MS analyses. On the other hand, the two candidate axial His ligands were protected from the modification due to a limited steric exposure of their imidazoles to solvent, the Fe^<3+>-N_<ε2> coordination bond, and the protonation of N_<δ2>81 by forming a hydrogen bond with their immediate surroundings. However, once N-carbethoxylation occurred at N_<ε2> of His97, resulting in a disruption of the heme Fe^<3+>-N_<ε2> coordination bond, it facilitated the second N-carbethoxylation to take place at N_<δ1> of the same imidazole ring, leading to a bis-N-carbethoxylated derivative and further to a ring-opened derivative. These phenomena were consistent with the bis-His68/His97 coordination. Further, these were not observed at all for cytochrome b_<561>, a transmembrane diheme containing protein responsible for the ascorbate-specific transmembrane electron transfer,where only a specific N_<δ1>-carbethoxylation of axial His occurred at a low concentration of DEPC,leading to an inhibition of the electron acceptance from ascorbate without a release of the heme.These distinct results might be related to a specific physiological mechanism being operative atthe cytosolic heme center of cytochrome b_<561>.

• 社団法人日本生物工学会の論文
• 2008-06-25

著者

• Hori Hiroshi

  Division of Biological Science, Graduate School of Science, Nagoya University

• Uno Tadayuki

  Division Of Analytical Chemistry Graduate School Of Pharmaceutical Sciences Osaka University

• Hori H

  Center For Quantum Science And Technology Under Extreme Conditions Osaka University

• Hori Hiroshi

  Division Of Biological Science Graduate School Of Science Nagoya University

• TSUBAKI Motonari

  Department of Life Science, Faculty of Science, Himeji Institute of Technology

• Hori Hiroshi

  Center For Quantum Science And Technology Under Extreme Conditions Osaka University

• Takeuchi Fusako

  Department of Pharmacy, College of Pharmaceutical Sciences, Ritsumeikan University

• NAKANISHI Nobuyuki

  Department of Molecular Science and Material Engineering, Graduate School of Science and Technology,

• Park Sam-Yong

  Division of Science of Biological Supramolecular Systems, Graduate School of Integrated Science, Yok

• Park Sam-yong

  Protein Design Lab. Yokohama City Univ.

• Kiyota Kohei

  Division of Analytical Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University

• Kiyota Kohei

  Division Of Analytical Chemistry Graduate School Of Pharmaceutical Sciences Osaka University

• Tsubaki M

  Department Of Chemistry Graduate School Of Science Kobe University

• Tsubaki Motonari

  Department Of Life Science Faculty Of Science Himeji Institute Of Technology

• Nakanishi Nobuyuki

  Department Of Molecular Science And Material Engineering Graduate School Of Science And Technology G

• Takeuchi Fusako

  Department Of Pharmacy College Of Pharmaceutical Sciences Ritsumeikan University

• Takeuchi Fusako

  Department Of Life Science Graduate School Of Science Himeji Institute Of Technology

• Hori Hiroshi

  Division Of Bioengineering Graduate School Of Engineering Science Osaka University

• Tsubaki Motonari

  Department Of Chemistry Graduate School Of Science Kobe University

• Park Sam-yong

  Protein Design Laboratory Department Of Supramolecular Biology Graduate School Of Nanobioscience Yok

• Tsubaki Motonari

  Departmemt of Chemistiy, Graduate School of Science, Kobe University

• NAKANISHI Nobuyuki

  Department of Chemistry, Graduate School of Science, Kobe University

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