Mössbauer spectroscopy of Fe/S proteins

Maria Eirini Pandelia, Nicholas D. Lanz, Squire J. Booker, Carsten Krebs

Research output: Contribution to journalReview article

36 Citations (Scopus)

Abstract

Iron-sulfur (Fe/S) clusters are structurally and functionally diverse cofactors that are found in all domains of life. 57Fe Mössbauer spectroscopy is a technique that provides information about the chemical nature of all chemically distinct Fe species contained in a sample, such as Fe oxidation and spin state, nuclearity of a cluster with more than one metal ion, electron spin ground state of the cluster, and delocalization properties in mixed-valent clusters. Moreover, the technique allows for quantitation of all Fe species, when it is used in conjunction with electron paramagnetic resonance (EPR) spectroscopy and analytical methods. 57Fe-Mössbauer spectroscopy played a pivotal role in unraveling the electronic structures of the "well-established" [2Fe-2S]2+/+, [3Fe-4S]1+/0, and [4Fe-4S]3+/2+/1+/0 clusters and -more-recently- was used to characterize novel Fe/S clustsers, including the [4Fe-3S] cluster of the O2-tolerant hydrogenase from Aquifex aeolicus and the 3Fe-cluster intermediate observed during the reaction of lipoyl synthase, a member of the radical SAM enzyme superfamily.

Original languageEnglish (US)
Pages (from-to)1395-1405
Number of pages11
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1853
Issue number6
DOIs
StatePublished - Jun 1 2015

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Protein S
Spectrum Analysis
Hydrogenase
Electron Spin Resonance Spectroscopy
Sulfur
Iron
Metals
Electrons
Ions
Enzymes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Pandelia, Maria Eirini ; Lanz, Nicholas D. ; Booker, Squire J. ; Krebs, Carsten. / Mössbauer spectroscopy of Fe/S proteins. In: Biochimica et Biophysica Acta - Molecular Cell Research. 2015 ; Vol. 1853, No. 6. pp. 1395-1405.
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Mössbauer spectroscopy of Fe/S proteins. / Pandelia, Maria Eirini; Lanz, Nicholas D.; Booker, Squire J.; Krebs, Carsten.

In: Biochimica et Biophysica Acta - Molecular Cell Research, Vol. 1853, No. 6, 01.06.2015, p. 1395-1405.

Research output: Contribution to journalReview article

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T1 - Mössbauer spectroscopy of Fe/S proteins

AU - Pandelia, Maria Eirini

AU - Lanz, Nicholas D.

AU - Booker, Squire J.

AU - Krebs, Carsten

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AB - Iron-sulfur (Fe/S) clusters are structurally and functionally diverse cofactors that are found in all domains of life. 57Fe Mössbauer spectroscopy is a technique that provides information about the chemical nature of all chemically distinct Fe species contained in a sample, such as Fe oxidation and spin state, nuclearity of a cluster with more than one metal ion, electron spin ground state of the cluster, and delocalization properties in mixed-valent clusters. Moreover, the technique allows for quantitation of all Fe species, when it is used in conjunction with electron paramagnetic resonance (EPR) spectroscopy and analytical methods. 57Fe-Mössbauer spectroscopy played a pivotal role in unraveling the electronic structures of the "well-established" [2Fe-2S]2+/+, [3Fe-4S]1+/0, and [4Fe-4S]3+/2+/1+/0 clusters and -more-recently- was used to characterize novel Fe/S clustsers, including the [4Fe-3S] cluster of the O2-tolerant hydrogenase from Aquifex aeolicus and the 3Fe-cluster intermediate observed during the reaction of lipoyl synthase, a member of the radical SAM enzyme superfamily.

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