Freeze-quench 57Fe-Mössbauer spectroscopy: Trapping reactive intermediates

Research output: Contribution to journalReview article

10 Citations (Scopus)

Abstract

57Fe-Mössbauer spectroscopy is a method that probes transitions between the nuclear ground state (I = 1/2) and the first nuclear excited state (I = 3/2). This technique provides detailed information about the chemical environment and electronic structure of iron. Therefore, it has played an important role in studies of the numerous iron-containing proteins and enzymes. In conjunction with the freeze-quench method, 57Fe-Mössbauer spectroscopy allows for monitoring changes of the iron site(s) during a biochemical reaction. This approach is particularly powerful for detection and characterization of reactive intermediates. Comparison of experimentally determined Mössbauer parameters to those predicted by density functional theory for hypothetical model structures can then provide detailed insight into the structures of reactive intermediates. We have recently used this methodology to study the reactions of various mononuclear non-heme-iron enzymes by trapping and characterizing several Fe(IV)-oxo reaction intermediates. In this article, we summarize these findings and demonstrate the potential of the method.

Original languageEnglish (US)
Pages (from-to)295-304
Number of pages10
JournalPhotosynthesis research
Volume102
Issue number2
DOIs
StatePublished - Nov 1 2009

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trapping
spectroscopy
Spectrum Analysis
Iron
Spectroscopy
iron
Reaction intermediates
Enzymes
Electron transitions
Model structures
methodology
Excited states
Ground state
Electronic structure
Density functional theory
chemical reactions
enzymes
electronics
Monitoring
monitoring

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Plant Science
  • Cell Biology

Cite this

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abstract = "57Fe-M{\"o}ssbauer spectroscopy is a method that probes transitions between the nuclear ground state (I = 1/2) and the first nuclear excited state (I = 3/2). This technique provides detailed information about the chemical environment and electronic structure of iron. Therefore, it has played an important role in studies of the numerous iron-containing proteins and enzymes. In conjunction with the freeze-quench method, 57Fe-M{\"o}ssbauer spectroscopy allows for monitoring changes of the iron site(s) during a biochemical reaction. This approach is particularly powerful for detection and characterization of reactive intermediates. Comparison of experimentally determined M{\"o}ssbauer parameters to those predicted by density functional theory for hypothetical model structures can then provide detailed insight into the structures of reactive intermediates. We have recently used this methodology to study the reactions of various mononuclear non-heme-iron enzymes by trapping and characterizing several Fe(IV)-oxo reaction intermediates. In this article, we summarize these findings and demonstrate the potential of the method.",
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Freeze-quench 57Fe-Mössbauer spectroscopy : Trapping reactive intermediates. / Krebs, Carsten; Bollinger, J. Martin.

In: Photosynthesis research, Vol. 102, No. 2, 01.11.2009, p. 295-304.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Freeze-quench 57Fe-Mössbauer spectroscopy

T2 - Trapping reactive intermediates

AU - Krebs, Carsten

AU - Bollinger, J. Martin

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N2 - 57Fe-Mössbauer spectroscopy is a method that probes transitions between the nuclear ground state (I = 1/2) and the first nuclear excited state (I = 3/2). This technique provides detailed information about the chemical environment and electronic structure of iron. Therefore, it has played an important role in studies of the numerous iron-containing proteins and enzymes. In conjunction with the freeze-quench method, 57Fe-Mössbauer spectroscopy allows for monitoring changes of the iron site(s) during a biochemical reaction. This approach is particularly powerful for detection and characterization of reactive intermediates. Comparison of experimentally determined Mössbauer parameters to those predicted by density functional theory for hypothetical model structures can then provide detailed insight into the structures of reactive intermediates. We have recently used this methodology to study the reactions of various mononuclear non-heme-iron enzymes by trapping and characterizing several Fe(IV)-oxo reaction intermediates. In this article, we summarize these findings and demonstrate the potential of the method.

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