Heme proteins and nitric oxide (NO): The neglected, eloquent chemistry in NO redox signaling and regulation

Douglas D. Thomas, Katrina M. Miranda, Carol A. Colton, Deborah Citrin, Michael Graham Espey, David A. Wink

Research output: Contribution to journalReview articlepeer-review

83 Scopus citations


The role of nitric oxide (NO) in cellular physiology and signaling has been an important aspect in biomedical science over the last decade. As NO is a small uncharged radical, the chemistry of NO within the redox environment of the cell dictates the majority of its biological effects. The mechanisms that have received the most attention from a biological perspective involve reactions with oxygen and superoxide, despite the rich literature of metal-NO chemistry. However, NO and its related species participate in important chemistry with metalloproteins. In addition to the well known direct interactions of NO with heme proteins such as soluble guanylate cyclase and oxyhemoglobin, there is much important, but often underappreciated, chemistry between other nitrogen oxides and heme/metal proteins. Here the basic chemistry of nitrosylation and the interactions of NO and other nitrogen oxides with metal-oxo species such as found in peroxidases and monoxygenases are discussed.

Original languageEnglish (US)
Pages (from-to)307-317
Number of pages11
JournalAntioxidants and Redox Signaling
Issue number3
StatePublished - Jun 2003

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology


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