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Title: Spectroscopic Evidence for a High-Spin Br-Fe(IV)-Oxo Intermediate in the alpha-Ketoglutarate-Dependent Halogenase CytC3 from Streptomyces

Abstract

The complex of the mononuclear non-heme halogenase CytC3 from Streptomyces, Fe(II), {alpha}-ketoglutarate, bromide, and the substrate l-2-aminobutyryl-S-CytC2 reacts with O2 to form a reaction intermediate. Variable-field, freeze-quench Mossbauer 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-Angstroms interaction between the Fe and one of its ligands is attributed to the Fe(IV)-oxo group, and a 2.43-Angstroms interaction is assigned to the Fe-Br interaction. A significantly longer Fe-Br separation (2.53 Angstroms) 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 {alpha}-ketoglutarate-dependent dioxygenases and halogenases.

Authors:
; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
959764
Report Number(s):
BNL-82750-2009-JA
Journal ID: ISSN 0002-7863; JACSAT; TRN: US201016%%908
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of the American Chemical Society; Journal Volume: 129
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; ABSORPTION SPECTROSCOPY; MIXTURES; PROTEINS; REACTION INTERMEDIATES; SPECTROSCOPY; STREPTOMYCES; SUBSTRATES; national synchrotron light source

Citation Formats

Galonic Fujimori,D., Barr, E., Matthews, M., Koch, G., Yonce, J., Walsh, C., Bollinger, J., Krebs, C., and Riggs-Gelasco, P. Spectroscopic Evidence for a High-Spin Br-Fe(IV)-Oxo Intermediate in the alpha-Ketoglutarate-Dependent Halogenase CytC3 from Streptomyces. United States: N. p., 2007. Web. doi:10.1021/ja076454e.
Galonic Fujimori,D., Barr, E., Matthews, M., Koch, G., Yonce, J., Walsh, C., Bollinger, J., Krebs, C., & Riggs-Gelasco, P. Spectroscopic Evidence for a High-Spin Br-Fe(IV)-Oxo Intermediate in the alpha-Ketoglutarate-Dependent Halogenase CytC3 from Streptomyces. United States. doi:10.1021/ja076454e.
Galonic Fujimori,D., Barr, E., Matthews, M., Koch, G., Yonce, J., Walsh, C., Bollinger, J., Krebs, C., and Riggs-Gelasco, P. Mon . "Spectroscopic Evidence for a High-Spin Br-Fe(IV)-Oxo Intermediate in the alpha-Ketoglutarate-Dependent Halogenase CytC3 from Streptomyces". United States. doi:10.1021/ja076454e.
@article{osti_959764,
title = {Spectroscopic Evidence for a High-Spin Br-Fe(IV)-Oxo Intermediate in the alpha-Ketoglutarate-Dependent Halogenase CytC3 from Streptomyces},
author = {Galonic Fujimori,D. and Barr, E. and Matthews, M. and Koch, G. and Yonce, J. and Walsh, C. and Bollinger, J. and Krebs, C. and Riggs-Gelasco, P.},
abstractNote = {The complex of the mononuclear non-heme halogenase CytC3 from Streptomyces, Fe(II), {alpha}-ketoglutarate, bromide, and the substrate l-2-aminobutyryl-S-CytC2 reacts with O2 to form a reaction intermediate. Variable-field, freeze-quench Mossbauer 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-Angstroms interaction between the Fe and one of its ligands is attributed to the Fe(IV)-oxo group, and a 2.43-Angstroms interaction is assigned to the Fe-Br interaction. A significantly longer Fe-Br separation (2.53 Angstroms) 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 {alpha}-ketoglutarate-dependent dioxygenases and halogenases.},
doi = {10.1021/ja076454e},
journal = {Journal of the American Chemical Society},
number = ,
volume = 129,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}