Proteins Containing 4Fe-4S Clusters: An Overview

Sweeney, William V.; Rabinowitz, Jesse C.

doi:10.1146/annurev.bi.49.070180.001035

Cited by 133 publications

(113 citation statements)

References 38 publications

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“…1B). In comparison, the [1Fe] system of rubredoxin exhibited only the Curie behavior, suggesting that holo-KpFeoC may possess a higher-order Fe-S cluster (30)(31)(32), consistent with the X-ray absorption results (see below).…”

Section: Resultssupporting

confidence: 81%

FeoC from Klebsiella pneumoniae Contains a [4Fe-4S] Cluster

Hsueh

Chen

et al. 2013

J Bacteriol

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Iron is essential for pathogen survival, virulence, and colonization. Feo is suggested to function as the ferrous iron (Fe 2؉ ) transporter. The enterobacterial Feo system is composed of 3 proteins: FeoB is the indispensable component and is a large membrane protein likely to function as a permease; FeoA is a small Src homology 3 (SH3) domain protein that interacts with FeoB; FeoC is a winged-helix protein containing 4 conserved Cys residues in a sequence suitable for harboring a putative iron-sulfur (Fe-S) cluster. The presence of an iron-sulfur cluster on FeoC has never been shown experimentally. We report that under anaerobic conditions, the recombinant Klebsiella pneumoniae FeoC (KpFeoC) exhibited hyperfine-shifted nuclear magnetic resonance (NMR) and a UV-visible (UV-Vis) absorbance spectrum characteristic of a paramagnetic center. The electron paramagnetic resonance (EPR) and extended X-ray absorption fine structure (EXAFS) results were consistent only with the [4Fe-4S] clusters. Substituting the cysteinyl sulfur with oxygen resulted in significantly reduced cluster stability, establishing the roles of these cysteines as the ligands for the Fe-S cluster. When exposed to oxygen, the [4Fe-4S] cluster degraded to [3Fe-4S] and eventually disappeared. We propose that KpFeoC may regulate the function of the Feo transporter through the oxygen-or iron-sensitive coordination of the Fe-S cluster.

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Section: Resultssupporting

confidence: 81%

FeoC from Klebsiella pneumoniae Contains a [4Fe-4S] Cluster

Hsueh

Chen

et al. 2013

J Bacteriol

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“…In agreement with previous studies (22,23), a single redox wave, with a midpoint potential of Ϫ369 Ϯ 4 mV, is observed between Ϫ300 and Ϫ600 mV. Moreover, the disappearance of all spectral features associated with oxidized clusters indicates that the two clusters of this protein display the same potential, as expected from a number of previous experiments (24).…”

Section: Circular Dichroism Spectroscopysupporting

confidence: 92%

“…The decrease of absorbance at 425 nm is a measure of the degree of reduction of [4Fe-4S] 2ϩ/ϩ clusters, as the spectra of the reduced clusters are less intense than those of the oxidized ones (24). Fig.…”

Section: Visible Absorption Spectroscopymentioning

confidence: 99%

The Two [4Fe-4S] Clusters in Chromatium vinosumFerredoxin Have Largely Different Reduction Potentials

Kyritsis¹,

Hatzfeld²,

Link³

et al. 1998

Journal of Biological Chemistry

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“…The UV-visible spectrum of the D-L(His) heterodimer contained absorbance maxima centered at 320 and 390 nm in addition to 280 nm (Fig. 4), consistent with the presence of Fe-S clusters (25). Although M. acetivorans subunit D is predicted to contain two [4Fe-4S] clusters, the A 390 /A 280 ratio is low, and the experimentally determined iron and acid-labile sulfide contents of as-purified D-L(His) heterodimer is substantially less than predicted ( Table 1 …”

Section: Archaealmentioning

confidence: 61%