Mössbauer spectroscopy of Fe/S proteins

Biochim Biophys Acta. 2015 Jun;1853(6):1395-405. doi: 10.1016/j.bbamcr.2014.12.005. Epub 2014 Dec 10.


Iron-sulfur (Fe/S) clusters are structurally and functionally diverse cofactors that are found in all domains of life. (57)Fe 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. (57)Fe-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.

Keywords: EPR spectroscopy; Fe/S clusters; Mossbauer spectroscopy.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Algorithms
  • Iron / chemistry*
  • Iron / metabolism
  • Iron-Sulfur Proteins / chemistry*
  • Iron-Sulfur Proteins / metabolism
  • Models, Chemical
  • Models, Molecular
  • Oxidation-Reduction
  • Protein Conformation
  • Spectroscopy, Mossbauer / methods*
  • Sulfur / chemistry*
  • Sulfur / metabolism


  • Iron-Sulfur Proteins
  • Sulfur
  • Iron