Studies of copper(ii)-binding to bacterioferritin and its effect on iron(ii) oxidationBased on the presentation given at Dalton Discussion No. 4, 10–13th January 2002, Kloster Banz, Germany.

Baaghil, Suzanne; Thomson, Andrew J.; Moore, Geoffrey R.; Brun, Nick E. Le

doi:10.1039/b107288a

Cited by 15 publications

(12 citation statements)

References 31 publications

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“…7A). This is consistent with the inhibitory effect these elements have on ferroxidase activity35363738; Cu however is usually reported to enhance the ferroxidase activity39. As for Ca and Mg, they showed a potentiation of the light production, especially for Ca although not statistically significant (135.7 ± 30.5%; P = 0.2609).…”

Section: Resultssupporting

confidence: 76%

Evidence that ferritin is associated with light production in the mucus of the marine worm Chaetopterus

Rawat

Deheyn

2016

Sci Rep

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The blue glow of the mucus from Chaetopterus involves a photoprotein, iron and flavins. Identity and respective role of these components remain, however, largely unresolved today, likely because of viscosity issues and inhibition of this system by oxidizers conventionally used to track bioluminescence activity. Here, we used gentle centrifugation to obtain a mucus supernatant showing no inhibition to oxidizers, allowing for further analysis. We applied conventional chromatographic techniques to isolate major proteins associated with light emission. Luminescence ability of elutriate fractions was tested with hydrogen peroxide to track photoprotein and/or protein-bound chromophore. Fractions producing light contained few major proteins, one with similarity to ferritin. Addition to the mucus of elements with inhibitory/potentiary effect on ferritin ferroxidase activity induced corresponding changes in light production, emphasizing the possible role of ferritin in the worm bioluminescence. DNA of the protein was cloned, sequenced, and expressed, confirming its identity to a Chaetopterus Ferritin (ChF). Both ferric and ferrous iron were found in the mucus, indicating the occurrence of both oxidase and reductase activity. Biochemical analysis showed ChF has strong ferroxidase activity, which could be a source of biological iron and catalytic energy for the worm bioluminescence when coupled to a reduction process with flavins.

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Section: Resultssupporting

confidence: 76%

Evidence that ferritin is associated with light production in the mucus of the marine worm Chaetopterus

Rawat

Deheyn

2016

Sci Rep

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“…Previously, it has been demonstrated that addition of copper(II) enhances the rate of core formation in wild-type EcBFR and that the effect of copper is associated with the protein, but independent of the ferroxidase center (23). It was also shown that copper(II) can restore iron(II)-oxidation activity to zinc(II)-inhibited EcBFR, consistent with the effect of copper(II) being independent of the ferroxidase center.…”

Section: Restoration Of Ferroxidase Activity In Ferroxidase Centerdefmentioning

confidence: 84%

Core Formation in Escherichia coli Bacterioferritin Requires a Functional Ferroxidase Center

et al. 2003

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Bacterioferritin from Escherichia coli is able to accumulate large quantities of iron in the form of an inorganic iron(III) mineral core. Core formation in the wild-type protein and a number of ferroxidase center variants was studied to determine key features of the core formation process and, in particular, the role played by the ferroxidase center. Core formation rates were found to be iron(II)-dependent and also depended on the amount of iron already present in the core, indicating the importance of the core surface in the mineralization reaction. Core formation was also found to be pH-dependent in terms of both rate and iron-loading characteristics, occurring with maximum efficiency at pH 6.5. Even at this optimum pH, however, the effective iron capacity was approximately 2700 per molecule, i.e., well below the theoretical limit of approximately 4500, suggesting that competing oxidation/precipitation processes have a major influence on the amount of iron accumulated. Disruption of the ferroxidase center, by site-directed mutagenesis or by chemical inhibition with zinc(II), had a profound effect on core formation. Effective iron capacities were found to be linked to iron(II) oxidation rates, and in zinc(II)-inhibited wild-type and E18A bacterioferritins core formation was severely restricted. Zinc(II) was also able, even at low stoichiometries (12-60 ions/protein), to significantly inhibit further core formation in protein already containing a substantial core, indicating the importance of the ferroxidase center throughout the core formation process. A mechanism is proposed that incorporates essential roles for the core surface and the ferroxidase center. A central feature of this mechanism is that dioxygen cannot readily gain access to the core, perhaps because the channels through the bacterioferritin coat are hydrophilic and dioxygen is nonpolar.

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“…Previous reports have demonstrated that the hydrophilic 3-fold channel of ferritin can also allow the transport of various other divalent metal ions, e.g., Cu 2+ , Co 2+ , and others, in addition to the uptake of Fe 2+ ions ( Tosha et al, 2010 ; Maity et al, 2019 ). Although the binding interactions of distinct ferritins with other metal ions vary considerably, the other ions can have noticeable effects on the structure and function of ferritins ( McKnight et al, 1997 ; Baaghil et al, 2002 ; Ardini et al, 2018 ). Notably, previous researches had revealed that these transition metal cations binding in ferritin could selectively inhibit ferritin enzyme activity, mainly by blocking Fe 2+ ion access, and the order of metal ion–protein binding stabilities was Mn 2+ << Co 2+ < Cu 2+ < Zn 2+ ion ( McKnight et al, 1997 ; Behera and Theil, 2014 ).…”

Section: Introductionmentioning

confidence: 99%

“…Among them, Cu 2+ ion has been demonstrated to have an important effect on the capability of iron oxidation at the ferroxidase site in ferritins. Baaghil et al reported that the presence of Cu 2+ ion was found to significantly enhance the rate of Fe 2+ ion oxidation and subsequent core formation ( Baaghil et al, 2002 ). McKnight et al (1997) found that Cu 2+ ion could bind tightly to horse spleen apoferritin, and had a catalytic effect on the aerobic oxidative uptake of Fe 2+ ion.…”

Section: Introductionmentioning

confidence: 99%

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa

Ming

Jiang

Huo

et al. 2022

Front. Mol. Biosci.

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In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu2+ ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper in recombinant Tegillarca granosa ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe2+ and Cu2+ ions on the TgFer structure and catalytic activity. The crystal structure revealed that TgFer presented a typically 4–3–2 symmetry in a cage-like, spherical shell composed of 24 identical subunits, featuring highly conserved organization in both the ferroxidase center and the 3-fold channel. Structural and biochemical analyses indicated that the 4-fold channel of TgFer could be serviced as potential binding sites of metal ions. Cu2+ ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe2+ ions, possibly inhibiting the ferroxidase activity of TgFer. Our results present a structural and functional characterization of TgFer, providing mechanistic insight into the interactions between TgFer and both Fe2+ and Cu2+ ions.

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Studies of copper(ii)-binding to bacterioferritin and its effect on iron(ii) oxidationBased on the presentation given at Dalton Discussion No. 4, 10–13th January 2002, Kloster Banz, Germany.

Cited by 15 publications

References 31 publications

Evidence that ferritin is associated with light production in the mucus of the marine worm Chaetopterus

Evidence that ferritin is associated with light production in the mucus of the marine worm Chaetopterus

Core Formation in Escherichia coli Bacterioferritin Requires a Functional Ferroxidase Center

Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa

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