Calculated and experimental spin state of seleno cytochrome p450

Yongying Jiang, Santhosh Sivaramakrishnan, Takahiro Hayashi, Shimrit Cohen, Pierre Moënneloccoz, Sason Shaik, Paul R. De Ortiz Montellano

Research output: Contribution to journalArticle

19 Scopus citations


A change for the better: The proximal cysteine thiolate in a cytochrome P450 enzyme is replaced by a selenocysteine. The resulting selenolate-ligated CYP119 protein has UV/Vis (see spectrum, ), EPR, and resonance Raman spectra that are similar to those of the native protein ( - ). These results are the first to fully describe a hemoprotein with a selenolate proximal ligand.

Original languageEnglish (US)
Pages (from-to)7193-7195
Number of pages3
JournalAngewandte Chemie - International Edition
Issue number39
StatePublished - Sep 14 2009


  • Cytochrome p450
  • Proteins
  • Raman spectroscopy
  • Selenium
  • Spin states

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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    Jiang, Y., Sivaramakrishnan, S., Hayashi, T., Cohen, S., Moënneloccoz, P., Shaik, S., & De Ortiz Montellano, P. R. (2009). Calculated and experimental spin state of seleno cytochrome p450. Angewandte Chemie - International Edition, 48(39), 7193-7195.