Reaction of cytochrome P450BM3 and peroxynitrite yields nitrosyl complex

Rachel K. Behan, Lee M. Hoffart, Kari L. Stone, Carsten Krebs, Michael T. Green

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Peroxynitrite has come into the spotlight in recent years. Its effects on proteins have been implicated in several diseases such as acute lung injury, rheumatoid arthritis, implant rejection, artherosclerosis, Parkinson's disease, and Alzheimer's disease. Peroxynitrite is thought to inactivate a variety of proteins including thiolate-ligated heme proteins such as cytochrome P450 2B1 and PGI2 synthase, through the nitration of tyrosine residues. In previous studies it was reported that thiolate-ligated heme enzymes react with peroxynitrite to form a ferryl intermediate. In an effort to spectroscopically characterize this species in P450BM3, we discovered that the peroxynitrite-generated intermediate is not an FeIVoxo, but rather an iron-nitrosyl {FeNO}6 complex. We present density functional calculations as well as Mossbauer and stopped-flow spectroscopic characterizations of the peroxynitrite-generated intermediate in P450 BM3.

Original languageEnglish (US)
Pages (from-to)5855-5859
Number of pages5
JournalJournal of the American Chemical Society
Volume129
Issue number18
DOIs
StatePublished - May 9 2007

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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