Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy

Carsten Krebs, Joseph M. Bollinger, Jr., Elizabeth C. Theil, Boi Hanh Huynh

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Oxygen activation at a carboxylate-bridged diiron cluster is employed by a number of enzymes for diverse biological functions. The mechanisms by which O2 is activated at the diferrous clusters have been studied in detail and peroxodiferric reaction intermediates have been observed in several of these diiron proteins. To understand further the magnetic properties of this common reaction intermediate, we have used Mössbauer spectroscopy to determine the magnitude and sign of the exchange coupling constant J (in the exchange Hamiltonian J S2 S2) of the peroxodiferric intermediates generated during the reactions of O2 with two different proteins, the recombinant M ferritin from frog and the site-directed variant W48F/D84E of the R2 subunit of ribonucleotide reductase from Escherichia coli. Both intermediates are antiferromagnetically coupled with a moderate coupling constant J of 50 ± 10 cm-1 for R2-W48F/D84E and 75 ± 10 cm-1 for M ferritin. This work demonstrates the capability of Mössbauer spectroscopy to determine exchange coupling constants of diiron complexes, including reaction intermediates. The approach and its limitations are described.

Original languageEnglish (US)
Pages (from-to)863-869
Number of pages7
JournalJournal of Biological Inorganic Chemistry
Volume7
Issue number7-8
DOIs
StatePublished - Dec 1 2002

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Reaction intermediates
Exchange coupling
Ferritins
Spectrum Analysis
Spectroscopy
Recombinant Proteins
Anura
Hamiltonians
Oxygen
Escherichia coli
Magnetic properties
Enzymes
Chemical activation
Proteins
ribonucleotide reductase R2 subunit

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

Cite this

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title = "Exchange coupling constant J of peroxodiferric reaction intermediates determined by M{\"o}ssbauer spectroscopy",
abstract = "Oxygen activation at a carboxylate-bridged diiron cluster is employed by a number of enzymes for diverse biological functions. The mechanisms by which O2 is activated at the diferrous clusters have been studied in detail and peroxodiferric reaction intermediates have been observed in several of these diiron proteins. To understand further the magnetic properties of this common reaction intermediate, we have used M{\"o}ssbauer spectroscopy to determine the magnitude and sign of the exchange coupling constant J (in the exchange Hamiltonian J S2 S2) of the peroxodiferric intermediates generated during the reactions of O2 with two different proteins, the recombinant M ferritin from frog and the site-directed variant W48F/D84E of the R2 subunit of ribonucleotide reductase from Escherichia coli. Both intermediates are antiferromagnetically coupled with a moderate coupling constant J of 50 ± 10 cm-1 for R2-W48F/D84E and 75 ± 10 cm-1 for M ferritin. This work demonstrates the capability of M{\"o}ssbauer spectroscopy to determine exchange coupling constants of diiron complexes, including reaction intermediates. The approach and its limitations are described.",
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Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy. / Krebs, Carsten; Bollinger, Jr., Joseph M.; Theil, Elizabeth C.; Huynh, Boi Hanh.

In: Journal of Biological Inorganic Chemistry, Vol. 7, No. 7-8, 01.12.2002, p. 863-869.

Research output: Contribution to journalArticle

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AB - Oxygen activation at a carboxylate-bridged diiron cluster is employed by a number of enzymes for diverse biological functions. The mechanisms by which O2 is activated at the diferrous clusters have been studied in detail and peroxodiferric reaction intermediates have been observed in several of these diiron proteins. To understand further the magnetic properties of this common reaction intermediate, we have used Mössbauer spectroscopy to determine the magnitude and sign of the exchange coupling constant J (in the exchange Hamiltonian J S2 S2) of the peroxodiferric intermediates generated during the reactions of O2 with two different proteins, the recombinant M ferritin from frog and the site-directed variant W48F/D84E of the R2 subunit of ribonucleotide reductase from Escherichia coli. Both intermediates are antiferromagnetically coupled with a moderate coupling constant J of 50 ± 10 cm-1 for R2-W48F/D84E and 75 ± 10 cm-1 for M ferritin. This work demonstrates the capability of Mössbauer spectroscopy to determine exchange coupling constants of diiron complexes, including reaction intermediates. The approach and its limitations are described.

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