2003
DOI: 10.1038/nsb909
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Abstract: The first crystal structure of a native di-iron center in an iron-storage protein (bacterio)ferritin is reported. The protein, isolated from the anaerobic bacterium Desulfovibrio desulfuricans, has the unique property of having Fe-coproporphyrin III as its heme cofactor. The three-dimensional structure of this bacterioferritin was determined in three distinct catalytic/redox states by X-ray crystallography (at 1.95, 2.05 and 2.35 A resolution), corresponding to different intermediates of the di-iron ferroxidas… Show more

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Cited by 106 publications
(195 citation statements)
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“…However, the relative populations of the Fe 3+ and Zn 2+ ions at the two sites apparently differ and are, thus, nonequivalent in this regard ( Figure 2). Nonequivalence at these sites, generally referred to as the A and B sites (9), has been observed previously (30)(31)(32). The zinc edge anomalous difference map shows a strong 24 σ peak at site A and a weaker 8 σ peak at site B, indicating significantly higher Zn 2+ occupancy at the A site compared to that of the B site.…”
Section: Bacterioferritin-like Metal Binding Sitesupporting
confidence: 64%
“…However, the relative populations of the Fe 3+ and Zn 2+ ions at the two sites apparently differ and are, thus, nonequivalent in this regard ( Figure 2). Nonequivalence at these sites, generally referred to as the A and B sites (9), has been observed previously (30)(31)(32). The zinc edge anomalous difference map shows a strong 24 σ peak at site A and a weaker 8 σ peak at site B, indicating significantly higher Zn 2+ occupancy at the A site compared to that of the B site.…”
Section: Bacterioferritin-like Metal Binding Sitesupporting
confidence: 64%
“…The structure has some important features different from those observed so far for other (bacterio)ferritins, such as the bacterioferritin from Desulfovibrio desulfuricans (DdBF) [11], and probably reveals a series of events relating to iron storage, including the shift of iron from ferroxidase center to the inner nucleation site and the selective entry of iron ions into the inner core through the fourfold channel.…”
Section: Introductionmentioning
confidence: 85%
“…Therefore, we consider that the heme preferentially binds to AvBF protein in one orientation, similar to the case of EcBF [17,21]. However, in the structures of both Rhodobacter capsulatus bacterioferritin (RcBF) [22] and DdBF [11], the heme groups were defined with two possible orientations each with an occupancy of about 0.50. Whether the heme group adopts two orientations or not perhaps depends on its interactions with surrounding residues.…”
Section: Orientation Of Heme Groupmentioning
confidence: 99%
“…The model is weakened by the absence of crystal structures of the mutant proteins, by the multiple sites for metal inhibitor binding in addition to the pores, and by studies suggesting other ferrous ion entry sites besides the gated pores [12,13]. In contrast, the model of ferrous ion transfer from the reduced mineral in the cavity through the gated pores is based on parallel structural studies in solution and crystals with functional studies in solution [3,14,15].…”
Section: Introductionmentioning
confidence: 99%