Identification of the ferroxidase centre in ferritin

Lawson, David M.; Treffry, Amyra; Artymiuk, Peter J.; Harrison, Pauline M.; Yewdall, S J; Luzzago, Alessandra; Cesareni, Gianne; Levi, Sonia; Arosio, Paolo

doi:10.1016/0014-5793(89)81040-3

Cited by 283 publications

(222 citation statements)

References 13 publications

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“…the N-terminal Met-1 [27]. The residues of the putative ferroxidase site in human H-ferritin are Glu-27, Glu-62, His-65, Glu-107, and Gln-141 [28]. In the bacterioferritins the corresponding amino acids are Glu-18, Glu-50, His-53, Glu-93, and Leu-119(Met).…”

Section: Resultsmentioning

confidence: 99%

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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Two distinct ferritin like iron containing proteins have been identified and isolated from the fungus Absidia spinosa; one from the spores and another from the mycelia. The mycelial protein has been purified and consists of two subunits of approx. 20 kDa. The N-terminal sequences of both subunits have been determined. The holoprotein as isolated contains approx. 750 iron atoms/molecule and exhibits a beme-like UV-Vis spectrum. Based on the beme spectrum and the high degree of sequence homology found, it has been established that the mycelial protein is a bacterioferritin. This is the first example demonstrating the presence of a bacterioferritin in a eukaryotic organism.

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Section: Resultsmentioning

confidence: 99%

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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“…Ions were generated by irradiating the sample area with a nitrogen laser at a wavelength of 337 nm. Calibrations were carried out using a mixture of angiotensin I (1297.51 MH + ), adrenocorticotropic hormone ACTH (clip [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17] …”

Section: Ms Analysismentioning

confidence: 99%

“…Accordingly, the H and L subunits have distinct and complementary functions. The H chains contain in the four-helix bundle a dinuclear ferroxidase center, which promotes the oxidation of Fe 2+ in the presence of molecular oxygen [7]. The iron ligands are highly conserved and are provided by residues E27, E61, E62, H65, E107 and Q141 [7].…”

mentioning

confidence: 99%

“…The H chains contain in the four-helix bundle a dinuclear ferroxidase center, which promotes the oxidation of Fe 2+ in the presence of molecular oxygen [7]. The iron ligands are highly conserved and are provided by residues E27, E61, E62, H65, E107 and Q141 [7]. The L chains lack such a center, but contain specific carboxylic groups (E57, E60, and E64 using the H-chain numbering) facing the inner surface of the apoferritin shell, that provide efficient nucleation sites for iron accumulation [8].…”

mentioning

confidence: 99%

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Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is an M‐type homopolymer

Mignogna¹,

Chiaraluce²,

Consalvi³

et al. 2002

European Journal of Biochemistry

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Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is composed of a single subunit that contains both the ferroxidase center residues, typical of mammalian H chains, and the carboxylate residues forming the micelle nucleation site, typical of mammalian L chains. Comparison of the amino-acid sequence with those available from lower vertebrates indicates that T. bernacchii ferritin can be classified as an M-type homopolymer. Interestingly, the T. bernacchii ferritin chain shows 85.7% identity with a coldinducible ferritin chain of the rainbow trout Salmo gairdneri. The structural and functional properties indicate that cold acclimation and functional adaptation to low temperatures are achieved without significant modification of the protein stability. In fact, the stability of T. bernacchii ferritin to denaturation induced by acid or temperature closely resembles that of mesophilic mammalian ferritins. Moreover iron is taken up efficiently and the activation energy of the reaction is 74.9 kJAEmol )1 , a value slightly lower than that measured for the human recombinant H ferritin (80.8 kJAEmol )1 ).

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“…In the Dps family, the ferrioxidase center is located at the twofold symmetry axis between two monomers rather than being embedded in the four-helix bundle of a single subunit in BFR. 14,20 So, although the monomer structures are similar, clearly, the underlying fundamentals that control the oligomer architecture and how these relate to the activity of these two subfamilies of protein cages are significantly different. Establishing the similarities and divergences in these proteins' structural energetics is an initial step in our long-term goal of converting, with a minimum of mutations, a mini-ferritin monomer into one that assembles into a maxi-ferritin and vice versa.…”

Section: Introductionmentioning

confidence: 99%

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

Zhang

Chee

et al. 2011

Protein Science

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DNA-binding protein from starved cells (DPS), a mini-ferritin capable of self-assembling into a 12-meric nano-cage, was chosen as the basis for an alanine-shaving mutagenesis study to investigate the importance of key amino acid residues, located at symmetry-related protein-protein interfaces, in controlling protein stability and self-assembly. Nine mutants were designed through simple inspection, synthesized, and subjected to transmission electron microscopy, circular dichroism, size exclusion chromatography, and ''virtual alanine scanning'' computational analysis. The data indicate that many of these residues may be hot spot residues. Most remarkably, two residues, R83 and R133, were observed to shift the oligomerization state to~50% dimer. Based on the hypothesis that these two residues constitute a ''hot strip,'' located at the ferritin-like threefold axis, the double mutant was generated which completely shuts down detectable formation of 12-mer in solution, favoring a cooperatively folded dimer. The fact that this effect logically builds upon the single mutants emphasizes that complex self-assembly has the potential to be manipulated rationally. This study should have an impact on the fundamental understanding of the assembly of DPS protein cages specifically and protein quaternary structure in general. In addition, as there is much interest in applying these and similar systems to the templation of nano-materials and drug delivery, the ability to control this ferritin's oligomerization state and stability could prove especially valuable.

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Identification of the ferroxidase centre in ferritin

Cited by 283 publications

References 13 publications

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Ferritin from the spleen of the Antarctic teleost Trematomus bernacchii is an M‐type homopolymer

Rational disruption of the oligomerization of the mini‐ferritin E. coli DPS through protein‐protein interface mutation

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