Evidence for two ferryl species in chloroperoxidase compound II

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

doi:10.1021/ja057876w

Evidence for two ferryl species in chloroperoxidase compound II

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

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76 Scopus citations

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 language	English (US)
Pages (from-to)	6147-6153
Number of pages	7
Journal	Journal of the American Chemical Society
Volume	128
Issue number	18
DOIs	https://doi.org/10.1021/ja057876w
State	Published - May 10 2006

All Science Journal Classification (ASJC) codes

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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title = "Evidence for two ferryl species in chloroperoxidase compound II",

abstract = "Using a combination of density functional calculations and M{\"o}ssbauer spectroscopy, we have examined chloroperoxidase compound II (CPO-II), The M{\"o}ssbauer 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 M{\"o}ssbauer 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.",

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T1 - Evidence for two ferryl species in chloroperoxidase compound II

AU - Stone, Kari L.

AU - Hoffart, Lee M.

AU - Behan, Rachel K.

AU - Krebs, Carsten

AU - Green, Michael T.

PY - 2006/5/10

Y1 - 2006/5/10

N2 - 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.

AB - 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.

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Evidence for two ferryl species in chloroperoxidase compound II

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