Spectroscopic evidence for a high-spin Br-Fe(IV)-OxO intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces

Danica Galonić Fujimori; Eric W. Barr; Megan L. Matthews; Gretchen M. Koch; J. Ryan Yonce; Christopher T. Walsh; J. Martin Bollinger; Carsten Krebs; Pamela J. Riggs-Gelasco

doi:10.1021/ja076454e

Spectroscopic evidence for a high-spin Br-Fe(IV)-OxO intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces

Danica Galonić Fujimori, Eric W. Barr, Megan L. Matthews, Gretchen M. Koch, J. Ryan Yonce, Christopher T. Walsh, J. Martin Bollinger, Carsten Krebs, Pamela J. Riggs-Gelasco

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Abstract

The complex of the mononuclear non-heme halogenase CytC3 from Streptomyces, Fe(II), α-ketoglutarate, bromide, and the substrate l-2-aminobutyryl-S-CytC2 reacts with O₂ to form a reaction intermediate. Variable-field, freeze-quench Mössbauer spectroscopy reveals this intermediate to be a mixture of two high-spin Fe(IV) complexes in an approximate 3.7/1 ratio. Freeze-quench Fe K-edge X-ray absorption spectroscopy provides further insight into the structure of this intermediate. A short 1.62-Å interaction between the Fe and one of its ligands is attributed to the Fe(IV)-oxo group, and a 2.43-Å interaction is assigned to the Fe-Br interaction. A significantly longer Fe-Br separation (2.53 Å) is observed in the reactant complex, consistent with lower valency of the Fe in the reactant complex. This intermediate is the first example for a Br-Fe(IV)-oxo complex in a protein and provides evidence for a unifying mechanism for Fe(II) and α-ketoglutarate-dependent dioxygenases and halogenases.

Original language	English (US)
Pages (from-to)	13408-13409
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	44
DOIs	https://doi.org/10.1021/ja076454e
State	Published - Nov 7 2007

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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Fujimori, D. G., Barr, E. W., Matthews, M. L., Koch, G. M., Yonce, J. R., Walsh, C. T., Bollinger, J. M., Krebs, C., & Riggs-Gelasco, P. J. (2007). Spectroscopic evidence for a high-spin Br-Fe(IV)-OxO intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces. Journal of the American Chemical Society, 129(44), 13408-13409. https://doi.org/10.1021/ja076454e

@article{04da8725719f457397033e8f56dc8d93,

title = "Spectroscopic evidence for a high-spin Br-Fe(IV)-OxO intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces",

abstract = "The complex of the mononuclear non-heme halogenase CytC3 from Streptomyces, Fe(II), α-ketoglutarate, bromide, and the substrate l-2-aminobutyryl-S-CytC2 reacts with O2 to form a reaction intermediate. Variable-field, freeze-quench M{\"o}ssbauer spectroscopy reveals this intermediate to be a mixture of two high-spin Fe(IV) complexes in an approximate 3.7/1 ratio. Freeze-quench Fe K-edge X-ray absorption spectroscopy provides further insight into the structure of this intermediate. A short 1.62-{\AA} interaction between the Fe and one of its ligands is attributed to the Fe(IV)-oxo group, and a 2.43-{\AA} interaction is assigned to the Fe-Br interaction. A significantly longer Fe-Br separation (2.53 {\AA}) is observed in the reactant complex, consistent with lower valency of the Fe in the reactant complex. This intermediate is the first example for a Br-Fe(IV)-oxo complex in a protein and provides evidence for a unifying mechanism for Fe(II) and α-ketoglutarate-dependent dioxygenases and halogenases.",

author = "Fujimori, {Danica Galoni{\'c}} and Barr, {Eric W.} and Matthews, {Megan L.} and Koch, {Gretchen M.} and Yonce, {J. Ryan} and Walsh, {Christopher T.} and Bollinger, {J. Martin} and Carsten Krebs and Riggs-Gelasco, {Pamela J.}",

year = "2007",

month = nov,

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doi = "10.1021/ja076454e",

language = "English (US)",

volume = "129",

pages = "13408--13409",

journal = "Journal of the American Chemical Society",

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T1 - Spectroscopic evidence for a high-spin Br-Fe(IV)-OxO intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces

AU - Fujimori, Danica Galonić

AU - Barr, Eric W.

AU - Matthews, Megan L.

AU - Koch, Gretchen M.

AU - Yonce, J. Ryan

AU - Walsh, Christopher T.

AU - Bollinger, J. Martin

AU - Krebs, Carsten

AU - Riggs-Gelasco, Pamela J.

PY - 2007/11/7

Y1 - 2007/11/7

N2 - The complex of the mononuclear non-heme halogenase CytC3 from Streptomyces, Fe(II), α-ketoglutarate, bromide, and the substrate l-2-aminobutyryl-S-CytC2 reacts with O2 to form a reaction intermediate. Variable-field, freeze-quench Mössbauer spectroscopy reveals this intermediate to be a mixture of two high-spin Fe(IV) complexes in an approximate 3.7/1 ratio. Freeze-quench Fe K-edge X-ray absorption spectroscopy provides further insight into the structure of this intermediate. A short 1.62-Å interaction between the Fe and one of its ligands is attributed to the Fe(IV)-oxo group, and a 2.43-Å interaction is assigned to the Fe-Br interaction. A significantly longer Fe-Br separation (2.53 Å) is observed in the reactant complex, consistent with lower valency of the Fe in the reactant complex. This intermediate is the first example for a Br-Fe(IV)-oxo complex in a protein and provides evidence for a unifying mechanism for Fe(II) and α-ketoglutarate-dependent dioxygenases and halogenases.

AB - The complex of the mononuclear non-heme halogenase CytC3 from Streptomyces, Fe(II), α-ketoglutarate, bromide, and the substrate l-2-aminobutyryl-S-CytC2 reacts with O2 to form a reaction intermediate. Variable-field, freeze-quench Mössbauer spectroscopy reveals this intermediate to be a mixture of two high-spin Fe(IV) complexes in an approximate 3.7/1 ratio. Freeze-quench Fe K-edge X-ray absorption spectroscopy provides further insight into the structure of this intermediate. A short 1.62-Å interaction between the Fe and one of its ligands is attributed to the Fe(IV)-oxo group, and a 2.43-Å interaction is assigned to the Fe-Br interaction. A significantly longer Fe-Br separation (2.53 Å) is observed in the reactant complex, consistent with lower valency of the Fe in the reactant complex. This intermediate is the first example for a Br-Fe(IV)-oxo complex in a protein and provides evidence for a unifying mechanism for Fe(II) and α-ketoglutarate-dependent dioxygenases and halogenases.

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Spectroscopic evidence for a high-spin Br-Fe(IV)-OxO intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces

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