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 language | English (US) |
|---|---|
| Pages (from-to) | 1395-1405 |
| Number of pages | 11 |
| Journal | Biochimica et Biophysica Acta - Molecular Cell Research |
| Volume | 1853 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jun 1 2015 |
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All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology
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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 journal › Review article
TY - JOUR
T1 - Mössbauer spectroscopy of Fe/S proteins
AU - Pandelia, Maria Eirini
AU - Lanz, Nicholas D.
AU - Booker, Squire J.
AU - Krebs, Carsten
PY - 2015/6/1
Y1 - 2015/6/1
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=84937107667&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84937107667&partnerID=8YFLogxK
U2 - 10.1016/j.bbamcr.2014.12.005
DO - 10.1016/j.bbamcr.2014.12.005
M3 - Review article
C2 - 25498248
AN - SCOPUS:84937107667
VL - 1853
SP - 1395
EP - 1405
JO - Biochimica et Biophysica Acta - Molecular Cell Research
JF - Biochimica et Biophysica Acta - Molecular Cell Research
SN - 0167-4889
IS - 6
ER -