Mossbauer spectroscopy of Fe/S proteins

被引：108

作者：

Pandelia, Maria-Eirini ^{[1
]}

Lanz, Nicholas D. ^{[2
]}

Booker, Squire J. ^{[1
,2
]}

Krebs, Carsten ^{[1
,2
]}

机构：

[1] Penn State Univ, Dept Chem, University Pk, PA 16802 USA

[2] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2015年 / 1853卷 / 06期

关键词：

Mossbauer spectroscopy; EPR spectroscopy; Fe/S clusters; IRON-SULFUR CLUSTERS; LYASE-ACTIVATING ENZYME; COLI BIOTIN SYNTHASE; BACTERIUM AQUIFEX-AEOLICUS; ELECTRON-PARAMAGNETIC-RES; SPIN-COUPLING MODEL; ESCHERICHIA-COLI; LIPOYL SYNTHASE; 4FE-4S CLUSTERS; RADICAL-SAM;

D O I：

10.1016/j.bbamcr.2014.12.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Iron-sulfur (Fe/S) clusters are structurally and functionally diverse cofactors that are found in all domains of life. Fe-57 Mossbauer 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. Fe-57-Mossbauer 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 O-2-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. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：1395 / 1405

页数：11

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