Rapid freeze-quench 57Fe Mössbauer spectroscopy: Monitoring changes of an iron-containing active site during a biochemical reaction

Carsten Krebs, John C. Price, Jeffrey Baldwin, Lana Saleh, Michael T. Green, Joseph M. Bollinger, Jr.

Research output: Contribution to journalReview article

98 Citations (Scopus)

Abstract

Nuclear gamma resonance spectroscopy, also known as Mössbauer spectroscopy, is a technique that probes transitions between the nuclear ground state and a low-lying nuclear excited state. The nucleus most amenable to Mössbauer spectroscopy is 57Fe, and 57Fe Mössbauer spectroscopy provides detailed information about the chemical environment and electronic structure of iron. Iron is by far the most structurally and functionally diverse metal ion in biology, and 57Fe Mössbauer spectroscopy has played an important role in the elucidation of its biochemistry. In this article, we give a brief introduction to the technique and then focus on two recent exciting developments pertaining to the application of 57Fe Mössbauer spectroscopy in biochemistry. The first is the use of the rapid freeze-quench method in conjunction with Mössbauer spectroscopy to monitor changes at the Fe site during a biochemical reaction. This method has allowed for trapping and subsequent detailed spectroscopic characterization of reactive intermediates and thus has provided unique insight into the reaction mechanisms of Fe-containing enzymes. We outline the methodology using two examples: (1) oxygen activation by the non-heme diiron enzymes and (2) oxygen activation by taurine:α- ketoglutarate dioxygenase (TauD). The second development concerns the calculation of Mössbauer parameters using density functional theory (DFT) methods. By using the example of TauD, we show that comparison of experimental Mössbauer parameters with those obtained from calculations on model systems can be used to provide insight into the structure of a reaction intermediate.

Original languageEnglish (US)
Pages (from-to)742-757
Number of pages16
JournalInorganic chemistry
Volume44
Issue number4
DOIs
StatePublished - Feb 21 2005

Fingerprint

Iron
Spectroscopy
iron
Monitoring
spectroscopy
Dioxygenases
biochemistry
Biochemistry
Taurine
enzymes
Chemical activation
activation
Oxygen
Reaction intermediates
reaction intermediates
oxygen
Enzymes
Electron transitions
biology
Excited states

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

Cite this

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title = "Rapid freeze-quench 57Fe M{\"o}ssbauer spectroscopy: Monitoring changes of an iron-containing active site during a biochemical reaction",
abstract = "Nuclear gamma resonance spectroscopy, also known as M{\"o}ssbauer spectroscopy, is a technique that probes transitions between the nuclear ground state and a low-lying nuclear excited state. The nucleus most amenable to M{\"o}ssbauer spectroscopy is 57Fe, and 57Fe M{\"o}ssbauer spectroscopy provides detailed information about the chemical environment and electronic structure of iron. Iron is by far the most structurally and functionally diverse metal ion in biology, and 57Fe M{\"o}ssbauer spectroscopy has played an important role in the elucidation of its biochemistry. In this article, we give a brief introduction to the technique and then focus on two recent exciting developments pertaining to the application of 57Fe M{\"o}ssbauer spectroscopy in biochemistry. The first is the use of the rapid freeze-quench method in conjunction with M{\"o}ssbauer spectroscopy to monitor changes at the Fe site during a biochemical reaction. This method has allowed for trapping and subsequent detailed spectroscopic characterization of reactive intermediates and thus has provided unique insight into the reaction mechanisms of Fe-containing enzymes. We outline the methodology using two examples: (1) oxygen activation by the non-heme diiron enzymes and (2) oxygen activation by taurine:α- ketoglutarate dioxygenase (TauD). The second development concerns the calculation of M{\"o}ssbauer parameters using density functional theory (DFT) methods. By using the example of TauD, we show that comparison of experimental M{\"o}ssbauer parameters with those obtained from calculations on model systems can be used to provide insight into the structure of a reaction intermediate.",
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Rapid freeze-quench 57Fe Mössbauer spectroscopy : Monitoring changes of an iron-containing active site during a biochemical reaction. / Krebs, Carsten; Price, John C.; Baldwin, Jeffrey; Saleh, Lana; Green, Michael T.; Bollinger, Jr., Joseph M.

In: Inorganic chemistry, Vol. 44, No. 4, 21.02.2005, p. 742-757.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Rapid freeze-quench 57Fe Mössbauer spectroscopy

T2 - Monitoring changes of an iron-containing active site during a biochemical reaction

AU - Krebs, Carsten

AU - Price, John C.

AU - Baldwin, Jeffrey

AU - Saleh, Lana

AU - Green, Michael T.

AU - Bollinger, Jr., Joseph M.

PY - 2005/2/21

Y1 - 2005/2/21

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AB - Nuclear gamma resonance spectroscopy, also known as Mössbauer spectroscopy, is a technique that probes transitions between the nuclear ground state and a low-lying nuclear excited state. The nucleus most amenable to Mössbauer spectroscopy is 57Fe, and 57Fe Mössbauer spectroscopy provides detailed information about the chemical environment and electronic structure of iron. Iron is by far the most structurally and functionally diverse metal ion in biology, and 57Fe Mössbauer spectroscopy has played an important role in the elucidation of its biochemistry. In this article, we give a brief introduction to the technique and then focus on two recent exciting developments pertaining to the application of 57Fe Mössbauer spectroscopy in biochemistry. The first is the use of the rapid freeze-quench method in conjunction with Mössbauer spectroscopy to monitor changes at the Fe site during a biochemical reaction. This method has allowed for trapping and subsequent detailed spectroscopic characterization of reactive intermediates and thus has provided unique insight into the reaction mechanisms of Fe-containing enzymes. We outline the methodology using two examples: (1) oxygen activation by the non-heme diiron enzymes and (2) oxygen activation by taurine:α- ketoglutarate dioxygenase (TauD). The second development concerns the calculation of Mössbauer parameters using density functional theory (DFT) methods. By using the example of TauD, we show that comparison of experimental Mössbauer parameters with those obtained from calculations on model systems can be used to provide insight into the structure of a reaction intermediate.

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JF - Inorganic Chemistry

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