Desulfovibrio vulgaris bacterioferritin uses H(2)O(2) as a co-substrate for iron oxidation and reveals DPS-like DNA protection and binding activities.

@article{Timteo2012DesulfovibrioVB,
  title={Desulfovibrio vulgaris bacterioferritin uses H(2)O(2) as a co-substrate for iron oxidation and reveals DPS-like DNA protection and binding activities.},
  author={Cristina G. Tim{\'o}teo and M{\'a}rcia Guilherme and Daniela Penas and Filipe Folgosa and Pedro Tavares and Alice S. Pereira},
  journal={The Biochemical journal},
  year={2012},
  volume={446 1},
  pages={
          125-33
        },
  url={https://api.semanticscholar.org/CorpusID:12774869}
}
It is proposed that D. vulgaris Bfr follows a mineralization mechanism similar to the one reported for vertebrate H-type ferritins subunits, in which a diferrous centre at the ferroxidase site is oxidized to diferric intermediate species, that are subsequently translocated into the inner nanocavity.
View on PubMed
biochemj.org
18 Citations
Background Citations
2

Figures from this paper

18 Citations

Dps–DNA interaction in Marinobacter hydrocarbonoclasticus protein: effect of a single-charge alteration

DNA-binding proteins from starved cells (Dps) are members of the ferritin family of proteins found in prokaryotes, with hollow rounded cube-like structures, composed of 12 equal subunits, which are associated with the N-terminal, positive charge rich, extensions that can promote DNA binding and condensation, apparently by a cooperative binding mechanism.

Campylobacter jejuni Dps Protein Binds DNA in the Presence of Iron or Hydrogen Peroxide

It is shown that the Campylobacter jejuni Dps has DNA binding activity that is uniquely activated by Fe(2+) or H2O2 at below neutral pH and was able to protect DNA in vitro from enzymatic cleavage and damage by hydroxyl radicals.

Unraveling the structure and function of bacterioferritin in Candidatus Kuenenia stuttgartiensis: Iron storage sites maintain cellular iron homeostasis.

Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin

The data indicate that the aromatic residues, together with a previously identified inner surface iron site, promote mineralization by ensuring the simultaneous delivery of two electrons, derived from Fe2+ oxidation in the BFR cavity, to the di‐ferric catalyst site for safe reduction of O2.

Spectroscopic evidence for the role of a site of the di-iron catalytic center of ferritins in tuning the kinetics of Fe(ii) oxidation.

It is observed that a site in the di-iron catalytic center controls the distribution of Fe(ii) among subunits of HuHF and PfFtn differently, which explains the reported differences in the kinetics of Fe (ii) oxidation and the amount of O2 consumed per Fe(II) oxidized.

Cryo-EM Structure of Bacterioferritin Nanocages Provides Insight into the Bio-mineralization of Ferritins

Three cryo-EM structures of different states of the Streptomyces coelicolor bacterioferritin nanocage are reported, revealing insight into its biomineralization and the potential channel for ferritin-associated iron trafficking.

Supramolecular protein polymers using mini-ferritin Dps as the building block.

A missense mutant of a Dps protein from Marinobacter hydrocarbonoclasticus was used as a building block to develop a new supramolecular assembly complex which enhances the iron uptake, a physiological function of this mini-ferritin.

Native hypersaline sulphate reducing bacteria contributes to iron nanoparticle formation in saltpan sediment: A concern for aquaculture.

Condensation and Protection of DNA by the Myxococcus xanthus Encapsulin: A Novel Function

The in vitro capacity of an encapsulin shell to interact and protect plasmid DNA similarly to other protein nanocages that may be relevant in vivo is reported for the first time.

UV radiation effects on a DNA repair enzyme: conversion of a [4Fe–4S]2+ cluster into a [2Fe–2S]2+

It is demonstrated that irradiation with a UV-C source has dramatic consequences on the absorption, fluorescence, structure and functionality of the protein, affecting its [4Fe–4S] cluster and its DNA-binding ability, which results in its inactivation.

53 References

Iron Detoxification Properties of Escherichia coliBacterioferritin

EPR spin trapping experiments show that the presence of EcBFR greatly attenuates the production of hydroxyl radical during Fe( II) oxidation by H2O2, consistent with the ability of the bacterioferritin to facilitate the pairwise oxidation of Fe(II) by H1O2.

Response of Desulfovibrio vulgaris Hildenborough to hydrogen peroxide: enzymatic and transcriptional analyses.

The data suggest that sod, sor, ngr and tpx genes, in addition to the PerR regulon, belong to the H( 2)O(2) stimulon.

The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants.

The rate of iron oxidation and the capacity to inhibit Fenton chemistry, thereby protecting DNA from oxidative damage, appear increasingly compromised, a further indication of the role of ferroxidation in conferring peroxide tolerance to the bacterium.

Iron and Hydrogen Peroxide Detoxification Properties of DNA-binding Protein from Starved Cells

The DNA-binding proteins from starved cells (Dps) are shown to be a Fe-binding and storage protein where Fe(II) oxidation is most effectively accomplished by H2O2 rather than by O2 as in ferritins, and the protective effect of Dps on DNA most likely is exerted through a dual action, the physical association with DNA and the ability to nullify the toxic combination of Fe( II) and H2 O2.

Binding of Pseudomonas aeruginosa apobacterioferritin-associated ferredoxin to bacterioferritin B promotes heme mediation of electron delivery and mobilization of core mineral iron.

Results from additional experimentation indicate that Bfd must bind to BFRB to promote heme mediation of electrons from the surface to the core to support the efficient mobilization of ferrous ions from BfrB.

Structural basis for iron mineralization by bacterioferritin.

X-ray crystallographic and kinetic methods support a model in which the ferroxidase center functions as a true catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins.

A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans ATCC 27774.

D. desulfuricans bacterioferritin appears to be the second example of a protein unexpectedly containing this heme cofactor, or a closely related porphyrin, after its finding in Desulfovibrio gigas rubredoxin:oxygen oxidoreductase.

Paired Bacillus anthracis Dps (Mini-ferritin) Have Different Reactivities with Peroxide*

Sequence similarities between Ba Dps1 and Bacillus subtilis DpsA (Dps1), which is regulated by general stress factor (SigmaB) and Fur, and betweenBa Dps2 and B. subtILis MrgA, which isregulated by H2O2 (PerR), suggest the function of Ba DPS1 is iron sequestration and thefunction of BaDps2 is H2 O2 destruction, important in host/pathogen interactions

Identification of the ferroxidase centre of Escherichia coli bacterioferritin.

Experiments report site-directed mutagenesis experiments based on a putative dinuclear-metal-ion-binding site located within the BFR subunit that reveals a metal-bound form of the centre that is identified as the ferroxidase centre of BFR.

Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center .

Structural observations suggest that the ferroxidase pore is the dominant entry route for the uptake of iron by Pa BfrB, and indicate that not all bacterioferritins operate in the same manner.
...