チオレート配位ヘム錯体の触媒活性に及ぼすNH・・・S水素結合の特異な効果

• 鈴木 潤

  名古屋市立大学大学院薬学研究科

• 山根 健浩

  名古屋市立大学大学院薬学研究科

• 梅澤 直樹

  名古屋市立大学大学院薬学研究科

• 加藤 信樹

  名古屋市立大学大学院薬学研究科

• 樋口 恒彦

  名古屋市立大学大学院薬学研究科

書誌事項

タイトル別名

• Anomalous Enhancing Effect of NH•••S Hydrogen Bonding on the Catalytic Activity of Heme Coordinated by Thiolate

抄録

Cytochrome P450 and NO synthase have strong oxidizing ability and unusual structure, in that their heme irons have thiolate coordination. Recently, the presence of an NH···S hydrogen bond in the active site of P450 and NOS has been confirmed. We have succeeded in the synthesis of the first synthetic heme thiolate (SR complex) which retains thiolate coordination during catalytic oxidation, and also have prepared heme thiolate having NH···S hydrogen bond (SR-HB complex). We have found that catalytic oxidizing activity of SR-HB is considerably higher than that of SR complex. We have also found that redox potential (Fe(III)/Fe(IV)) of SR-HB is lower than that of SR, contrary to expectation. This finding would involve function of NH···S hydrogen bond as a positive modulator of P450 catalysis.

収録刊行物

• 反応と合成の進歩シンポジウム 発表要旨概要

  反応と合成の進歩シンポジウム 発表要旨概要 35 (0), 27-27, 2009

  日本薬学会化学系薬学部会

キーワード

• cytochrome P450
• hydrogen bonding
• thiolate ligand
• iron porphyrin
• enzyme model

詳細情報

• CRID: 1390001205635787776
• NII論文ID: 130006998350
• DOI: 10.14895/hannou.35.0.27.0
• 本文言語コード: ja
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可