Evidence for two ferryl species in chloroperoxidase compound II

Kari L. Stone, Lee M. Hoffart, Rachel K. Behan, Carsten Krebs, Michael T. Green

Research output: Contribution to journalArticle

68 Citations (Scopus)

Abstract

Using a combination of density functional calculations and Mössbauer spectroscopy, we have examined chloroperoxidase compound II (CPO-II), The Mössbauer spectrum of CPO-II suggests the presence of two distinct ferryl species in an ∼70:30 ratio. Density functional calculations and cryogenic reduction and annealing experiments allow us to assign the major species as an Fe(IV)OH intermediate. The Mössbauer parameters of the minor component are indicative of an authentic iron(IV)oxo species, but we have found the 70:30 ratio to be pH invariant. The unchanging ratio of component concentrations is in agreement with CPO-II's visible absorption spectrum, which shows no change over the enzyme's range of pH stability.

Original languageEnglish (US)
Pages (from-to)6147-6153
Number of pages7
JournalJournal of the American Chemical Society
Volume128
Issue number18
DOIs
StatePublished - May 10 2006

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Chloride Peroxidase
Density functional theory
Cryogenics
Absorption spectra
Spectrum Analysis
Enzymes
Spectroscopy
Annealing
Iron
Experiments

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Stone, Kari L. ; Hoffart, Lee M. ; Behan, Rachel K. ; Krebs, Carsten ; Green, Michael T. / Evidence for two ferryl species in chloroperoxidase compound II. In: Journal of the American Chemical Society. 2006 ; Vol. 128, No. 18. pp. 6147-6153.
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Evidence for two ferryl species in chloroperoxidase compound II. / Stone, Kari L.; Hoffart, Lee M.; Behan, Rachel K.; Krebs, Carsten; Green, Michael T.

In: Journal of the American Chemical Society, Vol. 128, No. 18, 10.05.2006, p. 6147-6153.

Research output: Contribution to journalArticle

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AU - Hoffart, Lee M.

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AU - Green, Michael T.

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