Characterization of the oxygenated intermediate of the thermophilic cytochrome P450 CYP119

Ilia G. Denisov, Shao Ching Hung, Kara E. Weiss, Mark A. McLean, Yoshitsugu Shiro, Sam Yong Park, Paul M. Champion, Stephen G. Sligar

Research output: Contribution to journalArticlepeer-review

Abstract

Using UV-Vis, resonance Raman, and EPR spectroscopy we have studied the properties of the oxygenated ferrous cytochrome P450 from Sulfolobus Solfataricus, (CYP119). The recently determined crystal structure of CYP119 is compared with other available structures of P450s, and detailed structural and spectroscopic analyses are reported. With several structural similarities to CYP102, such as in-plane iron position and a shorter iron-proximal ligand bond, CYP119 shows low-spin conformation preference in the ferric form and partially in the ferrous form at low temperatures. These structural features can explain the fast autoxidation of the oxyferrous complex of CYP119. Finally, we report the first UV-Vis and EPR spectra of the cryoradiolytically reduced oxygenated intermediate of CYP119. The primary reduced intermediate, a hydroperoxo-ferric complex of CYP119, undergoes a 'peroxide shunt' pathway during gradual annealing at 170-195 K and returns to the low-spin ferric form.

Original languageEnglish (US)
Pages (from-to)215-226
Number of pages12
JournalJournal of Inorganic Biochemistry
Volume87
Issue number4
DOIs
StatePublished - Dec 15 2001

Keywords

  • Cryoradiolytic reduction
  • Cytochrome P450
  • Low temperature spectroscopy
  • Oxyferrous heme complex

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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