Characterization of iron coordination structure of nitric oxide reductase, cytochrome P450NOR

F. Ohayashi, Y. Shiro, S. Takahashi, F. Lizuka, H. Shoun

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1 Citation (Scopus)

Abstract

Cytochrome PloOnor (IMSOnor) cataly/rs the reduction of nitnc oxide to nitrous oxulo. but not the monooxvganation fraction, although it belongs to Itu1 P-ioO Miprrfamily. In order to elucidate what kind of defFerence in proIrin structure Mild coordination structure of the iron causes the functional differ encc. we niea.Mirrd infrared, resonance Raman and X-rav absorption spectra of P450nor, and compared them with those of P-iriOcain and otlirr hernoproteins. From these results, we found that the Fe-NO bond in the ferric state is st ronp,or than that of P450cam. This can be explainer] in l en us of the elect ron don at ion from the NO to the iron larger in IMoOnor than in Pl5Ucam. possibly due to difference in steric or electrostatic effect between NO and its .surroundings.

Original languageEnglish
Pages (from-to)A807
JournalFASEB Journal
Volume11
Issue number9
Publication statusPublished - 1997 Dec 1
Externally publishedYes

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

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