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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

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
Pages (from-to)7193-7195
Number of pages3
JournalAngewandte Chemie - International Edition
Volume48
Issue number39
DOIs
StatePublished - 14 Sep 2009

Keywords

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

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