Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies

Roman Davydov, Brian M. Hoffman

Research output: Contribution to journalReview articlepeer-review

45 Scopus citations

Abstract

This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.

Original languageEnglish (US)
Pages (from-to)36-43
Number of pages8
JournalArchives of biochemistry and biophysics
Volume507
Issue number1
DOIs
StatePublished - Mar 1 2011

Keywords

  • Cryoreduction
  • Cytochrome P450
  • Dioxygen activation
  • ENDOR
  • EPR
  • Heme oxygenase
  • Nitric oxide synthase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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