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1 ied within the four-helix bundle, similar to bacterioferritin.
2 hat they could provide a route for iron into bacterioferritin.
3 cinate dehydrogenase), and a gene encoding a bacterioferritin.
4 atios of several mammalian ferritins and one bacterioferritin.
5 alpha and beta, of the iron-binding protein, bacterioferritin.
6 xidation and hydrolysis chemistry in E. coli bacterioferritin.
7 es was not impaired by deletion of the alpha-bacterioferritin.
8 xidase center and the iron storage cavity of bacterioferritin.
9 f the protein to stimulate iron release from bacterioferritin.
10 ls (DPS)-like protein than to the 24-subunit bacterioferritins.
11 suggesting a new role(s) haem might play in bacterioferritins.
13 the recombinant M. smegmatis strain exported bacterioferritin, a large (approximately 500-kDa), leade
14 nucleation centers for the mineral cores in bacterioferritins and indicate that these proteins are n
15 acterial two-hybrid system screen identified bacterioferritins and the heme-containing subunit NarI o
16 which includes the 24 subunit ferritins and bacterioferritins, and 12 subunit mini-ferritins (DPS).
19 chocystis sp. PCC 6803 (Synechocystis 6803), bacterioferritins are responsible for the storage of as
21 Escherichia coli and Rhodobacter capsulatus bacterioferritins are unable to associate into 24-meric
22 the centre of a 4 alpha-helical bundle, but bacterioferritins are unique in also binding 12 hemes pe
23 eroxidase, the heat shock protein GroEL, and bacterioferritin as measured by splenic lymphocyte proli
24 as aeruginosa suggested the possibility of a bacterioferritin assembled from two different subunits.
25 presence of a "regulator", the apo form of a bacterioferritin-associated ferredoxin (apo Pa Bfd).
26 BfrB, FPR, and the apo form of P. aeruginosa bacterioferritin-associated ferredoxin (apo-Bfd) results
27 dehydratase (fumC), bacterioferritin (bfr), bacterioferritin-associated ferredoxin (bfd), and multip
28 a bacterioferritin (Pa-BfrB) in complex with bacterioferritin-associated ferredoxin (Pa-Bfd) at 2.0 A
31 ucture of recombinant Pseudomonas aeruginosa bacterioferritin B (Pa BfrB) has been determined from cr
33 , vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are
34 onstrated specific complex formation between bacterioferritin (Bfr) and this NIFU-like [2Fe-2S] prote
37 smutase (sodA), fumarate dehydratase (fumC), bacterioferritin (bfr), bacterioferritin-associated ferr
38 e fluorescence intensity of Escherichia coli bacterioferritin (BFR), due to the presence of two trypt
39 ation of a natural protein nanocage, E. coli bacterioferritin (Bfr), using synchrotron radiation smal
41 often coexist in bacteria, the heme binding bacterioferritins (Bfr) and the non-heme binding bacteri
43 many other cyanobacterial species, have two bacterioferritins, BfrA and BfrB, in which either the he
45 eroxiredoxins (alkylhydroperoxide reductase, bacterioferritin co-migratory protein and a thiol-peroxi
48 ecently reclassified one such peroxiredoxin, bacterioferritin comigratory protein (BCP) of Escherichi
49 0 in the catalytic cycle of Escherichia coli bacterioferritin comigratory protein (BCP), a previous s
54 ferroxidase center (FC) of Escherichia coli bacterioferritin (EcBfr) but mechanistic details of the
55 oxidized di-Fe(3+) site of Escherichia coli bacterioferritin (EcBFR) is stable and therefore does no
59 Although the structures consist of a typical bacterioferritin fold comprised of a nearly spherical 24
60 r between the heme and ferroxidase centre of bacterioferritin from Escherichia coli was recently demo
62 n open reading frame located upstream of the bacterioferritin gene in Escherichia coli encodes a hypo
64 ext, the thus far mysterious role of heme in bacterioferritins has been brought to the front by recon
67 l iron, thus demonstrating a central role of bacterioferritins in iron homeostasis in these photosynt
68 heteromultimeric structure of Synechocystis bacterioferritin, in which one subunit ligates a di-iron
71 r cytochrome with such a ligand arrangement, bacterioferritin, is too large to be studied by current
72 g from the exterior surface of SsDPSL to the bacterioferritin-like dimetal binding site, possibly all
75 nt role in the reductive mobilisation of the bacterioferritin mineral core, which is dependent on the
78 of the product of the bfrB gene as a genuine bacterioferritin (Pa BfrB), indicate the coexistence of
79 crystal structure of Pseudomonas aeruginosa bacterioferritin (Pa-BfrB) in complex with bacterioferri
82 es and the iron-activated genes encoding two bacterioferritins (PSPTO_0653 and PSPTO_4160), a ParA pr
83 oli (E. coli) multifunctional single subunit bacterioferritin recognized two proteins in the Pp extra
85 quired to maintain iron homeostasis, whereas bacterioferritin seems to be dispensable for this functi
88 ort the structure of Acinetobacter baumannii bacterioferritin, the first structural example of a hete
89 is acknowledged that the two iron motifs in bacterioferritins, the di-nuclear ferroxidase centre and
91 ) forms of the native Azotobacter vinelandii bacterioferritin to 2.7 and 2.0 A resolution, respective
92 H(2)O(2), consistent with the ability of the bacterioferritin to facilitate the pairwise oxidation of
94 te of the virulent clinical isolate, whereas bacterioferritin was more abundant in the culture filtra
95 34, Glu-66, Asp-132, and Asp-139) of E. coli bacterioferritin were substituted to determine if they a
96 e transcripts of the two bfr genes (encoding bacterioferritin) were found to be constitutively up-reg