Ferredoxins of the third kind

@article{Meyer2001FerredoxinsOT,
  title={Ferredoxins of the third kind},
  author={J. Meyer},
  journal={FEBS Letters},
  year={2001},
  volume={509}
}
  • J. Meyer
  • Published 30 November 2001
  • Chemistry
  • FEBS Letters
Thioredoxin‐Like [2Fe–2S] Ferredoxin
Thioredoxin-like [2Fe–2S] ferredoxin (Trx-like-Fd) is a soluble homodimer of ca. 100-residue subunits, each containing a [2Fe–2S] cluster. This cluster is redox active and shuttles between the
A bacteria-specific 2[4Fe-4S] ferredoxin is essential in Pseudomonas aeruginosa
TLDR
The gene of the very low potential 2[4Fe-4S] ferredoxin displays characteristics of a housekeeping gene, and it belongs to the minority of genes that are essential in Pseudomonas aeruginosa, a new potential antimicrobial target in this and other pathogenic Proteobacteria.
Adrenodoxin: the archetype of vertebrate-type [2Fe-2S] cluster ferredoxins.
A New Class of Thioredoxin-Related Protein Able to Bind Iron-Sulfur Clusters.
TLDR
It is demonstrated that IsTRP defines a new protein family within the Trx superfamily, the conservation of function for class II Grx from nonphylogenetically related species is confirmed, and the versatility of the TrX folding unit to acquire Fe/S binding as a recurrent emergent function is highlighted.
Arabidopsis thaliana DGAT3 is a [2Fe-2S] protein involved in TAG biosynthesis
TLDR
To date, AtDGAT3 is the first metalloprotein described as a DGAT, and the results obtained demonstrate the presence of a [2Fe-2S] cluster in the protein.
Identification of a new family of plant proteins loosely related to glutaredoxins with four CxxC motives
TLDR
The presence of a new protein family in higher plants, constituted of 19 members in Populus trichocarpa, 15 in Arabidopsis thaliana and 17 in Oryza sativa, which do not share the major conserved features of glutaredoxins but instead display four conserved CxxC motives.
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References

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Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus.
TLDR
The presence of homologs of this ferredoxin as components of more complex anaerobic and aerobic electron transfer systems indicates that this is a versatile fold for biological redox processes.
Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster.
TLDR
A combination of site-directed mutagenesis and UV-vis, EPR, and resonance Raman spectroscopy has been implemented to obtain information on the identity of the ligands of the iron-sulfur cluster.
Mutated forms of a [2Fe-2S] ferredoxin with serine ligands to the iron-sulfur cluster.
TLDR
The modified ferredoxins have been purified and were all found to contain a [2Fe-2S]-type cluster, and the electronic absorption and EPR spectra of the C24S protein were only slightly different from those of the native one.
A [2Fe-2S] protein from the hyperthermophilic bacterium Aquifex aeolicus.
Overexpression in Escherichia coli of the fdx4 gene from Aquifex aeolicus has allowed isolation and characterization of the first hyperthermophilic [2Fe-2S](Scys)(4) protein, a homodimer of M = 2 x
Coordination of the [2Fe-2S] Cluster in Wild Type and Molecular Variants of Clostridium pasteurianum Ferredoxin, Investigated by ESEEM Spectroscopy†
TLDR
The data shown here indicate that the fourth ligand of the [2Fe-2S] cluster is neither a histidine residue nor another nitrogenous ligand, and the possibility of oxygenic coordination for this molecular variant is discussed.
Crystal structure of the 2[4Fe‐4S] ferredoxin from Chromatium vinosum: Evolutionary and mechanistic inferences for [3/4Fe‐4S] ferredoxins
TLDR
The structure of C. vinosum ferredoxin strongly suggests divergent evolution for bacterial [3/4Fe‐4S] ferredoxins from a common ancestral cluster‐binding core and may be attributed to the unusual electronic properties of one of the clusters arising from localized changes in its vicinity rather than to a global structural rearrangement.
Extensive ligand rearrangements around the [2Fe-2S] cluster of Clostridium pasteurianum ferredoxin.
TLDR
The data provide an extensive confirmation that Fe-S clusters have a strong preference for thiolate ligation and rationalize the relatively rare occurrence of noncysteinyl ligation in native Fe- S proteins.
The evolution of ferredoxins.
  • J. Meyer
  • Biology, Chemistry
    Trends in ecology & evolution
  • 1988
Adrenodoxin: Structure, stability, and electron transfer properties
TLDR
The recently solved first crystal structure of the vertebrate‐type ferredoxin, the truncated adrenodoxin Adx(4‐108), is discussed, that offers the unique opportunity for better understanding of the structure‐function relationships and stabilization of this protein, as well as of the molecular architecture of [2Fe‐2S] ferredoxins in general.
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