Nitric Oxide Synthesis Capabilities of Cytochrome P450 1A2 and NADPH-Cytochrome P450 Reductase from <i>N</i> <i>G</i>-Hydroxy-<scp>l</scp>-Arginine

• Hiroaki Sano

  Institute for Chemical Reaction Science, Tohoku UniversitySendai

• Hideaki Sato

  Institute for Chemical Reaction Science, Tohoku UniversitySendai

• Ikuko Sagami

  Institute for Chemical Reaction Science, Tohoku UniversitySendai

• Toru Shimizu

  Institute for Chemical Reaction Science, Tohoku UniversitySendai

Abstract

NO was formed from NG-hydroxy-l-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 H2O2 or superoxide anion in the NO synthesis is also suggested.

Journal

• Chemistry Letters

  Chemistry Letters 26 (8), 759-760, 1997-08-01

  Oxford University Press (OUP)

Keywords

• General Chemistry

Details

• CRID: 1360846644039526784
• NII Article ID: 10002613824
• NII Book ID: AA00603318
• DOI: 10.1246/cl.1997.759
• ISSN: 13480715
• ISSN: 03667022
• Web Site: https://academic.oup.com/chemlett/article-pdf/26/8/759/56075446/cl.1997.759.pdf
• Data Source:
  • Crossref
  • CiNii Articles