Nitric Oxide Synthesis Capabilities of Cytochrome P450 1A2 and NADPH-Cytochrome P450 Reductase from N^G-Hydroxy-L-Arginine

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著者

    • SANO Hiroaki
    • Institute for Chemical Reaction Science, Tohoku University
    • SATO Hideaki
    • Institute for Chemical Reaction Science, Tohoku University
    • SAGAMI Ikuko
    • Institute for Chemical Reaction Science, Tohoku University
    • SHIMIZU Toru
    • Institute for Chemical Reaction Science, Tohoku University

抄録

NO was formed from <I>N</I><SUP><I>G</I></SUP>-hydroxy-<FONT SIZE=-2>L</FONT>-arginine by cytochrome P450 1A2 (P450 1A2) with turnover numbers of 0.6 - 1.2 nmol/nmolP450/min and 62 pmol/nmolP450/min in peroxide-supported shunt and reconstituted systems, respectively. A Glu318Ala mutation of P450 1A2 enhanced the shunt-reaction activity up to 7.3-fold, whereas the mutation abolished the activity with the reconstituted system. Involvement of H<SUB>2</SUB>O<SUB>2</SUB> or superoxide anion in the NO synthesis is also suggested.

収録刊行物

  • Chemistry letters

    Chemistry letters 1997(8), 759-760, 1997-08

    The Chemical Society of Japan

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各種コード

  • NII論文ID(NAID)
    10002613824
  • NII書誌ID(NCID)
    AA00603318
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    03667022
  • データ提供元
    CJP書誌  J-STAGE 
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