ライフサイエンスコーパス: ferroxidase

1 (ferrireductases) and ferrous iron oxidases (ferroxidases).

2 per-dependent enzymes like Cyt oxidase and a ferroxidase.

3 CRD2 in a pathway for copper delivery to the ferroxidase.

4 the Fet3 protein (Fet3p) was a cell surface ferroxidase.

5 multicopper oxidase-1 (MCO1) is a functional ferroxidase.

6 ogous to ceruloplasmin (Cp) in that both are ferroxidases.

7 iated with an upregulation of iron-exporting ferroxidases.

8 tions are distinct from those of other known ferroxidases.

9 m secondary iron deficiency owing to reduced ferroxidase abundance, suggesting a role for CRR1 in cop

10 mediated by ferritin is the oxidation at the ferroxidase active site of two ferrous ions to a diferri

11 The H chain contains a ferroxidase active site resembling that of vertebrate H

12 Sites A and B comprise the conserved ferroxidase active site, and site C forms a pathway lead

13 n also stimulated both the phenoloxidase and ferroxidase activities of the enzyme, but the other meta

14 erences in heme- and metal-binding sites and ferroxidase activities of the two types of subunits are

15 or retention of both p-phenylenediamine and ferroxidase activities, indicating that the ability of F

16 as demonstrated to exhibit phenoloxidase and ferroxidase activities.

17 erobic conditions was most likely due to its ferroxidase activity [with consequent reuptake of Fe(III

18 ontrast to HuHF, MtF does not regenerate its ferroxidase activity after oxidation of its initial comp

19 iseries reveal a maxi-ferritin that exhibits ferroxidase activity and binds iron.

20 (Cp) in iron metabolism is suggested by its ferroxidase activity and by the tissue iron overload in

21 In contrast, the assembled protein has ferroxidase activity and detoxifies redox-active iron by

22 s in paired Bacilli Dps protein, we measured ferroxidase activity and DNA protection (hydroxyl radica

23 reted by IFN-gamma-stimulated U937 cells had ferroxidase activity and was, in fact, the only secreted

24 e iron metabolism is suggested by its potent ferroxidase activity catalyzing conversion of Fe2+ to Fe

25 ltered at critical amino acids essential for ferroxidase activity could not restore wild-type catalas

26 monstrate that Hp has both amine oxidase and ferroxidase activity in cultured cells and primary intes

27 nd a approximately 80% loss of ceruloplasmin ferroxidase activity in the substantia nigra of idiopath

28 ith inhibitory/potentiary effect on ferritin ferroxidase activity induced corresponding changes in li

29 These observations indicate that the ferroxidase activity of Fet3p is intrinsically required

30 The ferroxidase activity of the ferritin H chain is critical

31 ar in nature, and their contributions to the ferroxidase activity of these proteins have been analyze

32 plasmin (Cp), a copper protein with a potent ferroxidase activity that converts Fe2+ to Fe3+ in the p

33 ere is still a question of whether it is the ferroxidase activity that is essential for iron transpor

34 The ferritin heavy chain (FtH) has ferroxidase activity that is required for iron incorpora

35 and Co(II) in the expected manner and shows ferroxidase activity under single turnover conditions.

36 Cp ferroxidase activity was required for iron uptake as sho

37 ease in volume (measured by gel filtration); ferroxidase activity was still in the millisecond range,

38 Regeneration of protein ferroxidase activity with time is observed for both HoSF

39 Both oligomeric forms of Dps-1 exhibit ferroxidase activity, and Fe(II) oxidation/mineralizatio

40 and chromosome compaction, metal chelation, ferroxidase activity, and regulation of gene expression.

41 We suggest that hephaestin, by way of its ferroxidase activity, facilitates iron export from intes

42 FtH, regardless of iron content and ferroxidase activity, induced FPN.

43 As shown here, Mn(II) inhibits ferroxidase activity, suggesting that ferroxidation may

44 tempt to generate Fet3p specifically lacking ferroxidase activity, we used site-directed mutagenesis

45 Biochemical analysis showed ChF has strong ferroxidase activity, which could be a source of biologi

46 may contribute to defense responses via its ferroxidase activity, which may drive iron homeostasis i

47 s Fpn-iron on cell surface in the absence of ferroxidase activity.

48 ther multicopper oxidases that are devoid of ferroxidase activity.

49 hCp) are members of this family that exhibit ferroxidase activity.

50 essing conserved amino acids responsible for ferroxidase activity.

51 ting DNA binding under conditions of ongoing ferroxidase activity.

52 rbated in spl7 and associated with a lack of ferroxidase activity.

53 oplasmin (Cp) is an acute-phase protein with ferroxidase, amine oxidase, and pro- and antioxidant act

54 In-gel and spectrophotometric ferroxidase and amine oxidase assays demonstrated that C

55 e elements of Fet3p that define it as both a ferroxidase and cuprous oxidase.

56 rotein since Glu61 is a shared ligand of the ferroxidase and nucleation sites of the protein.

57 th early work identifying ceruloplasmin as a ferroxidase and with recent findings showing an essentia

58 ionally interacting Arabidopsis genes, LPR1 (ferroxidase) and PDR2 (P5-type ATPase), are key players

59 ae requires a metal reductase, a multicopper ferroxidase, and an iron permease.

60 matory response, transition metal transport, ferroxidase, and presynaptic signaling activity, while C

61 s that work in concert with ferrireductases, ferroxidases, and chaperones to direct the movement of i

62 nal iron absorption and is predicted to be a ferroxidase based on significant sequence identity to th

63 Multicopper ferroxidases catalyze the oxidation of ferrous iron to f

64 s130 in this structure is rotated toward the ferroxidase center and coordinates an iron ion.

65 that in this mutant metal ion binding to the ferroxidase center and Fe(II) oxidation at this site was

66 n FeSO(4) solution displays a fully occupied ferroxidase center and iron bound to the internal, Fe((i

67 rface of each subunit in the vicinity of the ferroxidase center and is believed to be the path for Fe

68 s highly sensitive to the iron status of the ferroxidase center and is quenched to different extents

69 n into the protein shell, its binding at the ferroxidase center and its subsequent oxidation by O(2).

70 rates of initial oxidation of Fe(II) at the ferroxidase center and subsequent iron mineralization wa

71 s a major route for iron entry into both the ferroxidase center and the iron storage cavity of bacter

72 semble in a metal dependent manner to form a ferroxidase center at a dimer interface.

73 here [Fe(II)(2)-P](Z) represents a diferrous ferroxidase center complex of the protein P with net cha

74 annels that guide the Fe(II) ions toward the ferroxidase center directly through the protein shell an

75 ation and the rate at which Fe(3+) exits the ferroxidase center for storage within the mineral core.

76 ation, the data support a model in which the ferroxidase center functions as a true catalytic cofacto

77 of self-assembly for the functioning of the ferroxidase center has not been investigated.

78 The pathway of Fe(II) to the ferroxidase center has remained elusive, and the importa

79 that serine 144, a residue situated near the ferroxidase center in MtF but absent from HuHF, is one p

80 The ferroxidase center in the as-isolated, mineralized, and

81 That only one site of the ferroxidase center is occupied by Fe(2+) implies that Fe

82 Calorimetric titrations show that the ferroxidase center is the principal locus for Fe(2+) bin

83 ng center (sites A and B), homologous to the ferroxidase center of H-type ferritin, and an adjacent m

84 The di-iron catalytic ferroxidase center of PmFTN (sites A and B) has a nearby

85 by which the Fe(2+) travels to the dinuclear ferroxidase center prior to its oxidation to Fe(3+).

86 Mutation of ferroxidase center residues (E62K+H65G) eliminates the b

87 n, on the other hand, must rotate toward the ferroxidase center to coordinate iron.

88 path for the translocation of iron from the ferroxidase center to the interior cavity.

89 Ftns and clearly distinct from those of the ferroxidase center typical of Bfrs.

90 h following oxidation of Fe2+ to Fe3+ at the ferroxidase center was not observed, indicating that the

91 ing heme that harbors a catalytically active ferroxidase center with structural properties similar to

92 24 subunits, to a di-iron binding site, the ferroxidase center, buried in the middle of each active

93 nels do not facilitate O(2) transport to the ferroxidase center, contrary to predictions of DFT and m

94 lying approximately 10 A directly below the ferroxidase center, coordinated by only two residues, Hi

95 not completely prevent Fe(2+) binding to the ferroxidase center, iron gains access to the center in a

96 intrasubunit catalytic center, known as the ferroxidase center, is preformed, ready to accept Fe(2+)

97 p133, which lies approximately 10 A from the ferroxidase center, is primarily responsible for the obs

98 here on the protein and that one site of the ferroxidase center, likely the His65 containing A-site,

99 oxidation of two Fe(II) per H(2)O(2) at the ferroxidase center, thus avoiding hydroxyl radical produ

100 is believed to be the path for Fe(II) to the ferroxidase center, was not disrupted.

101 ole, possibly serving to recycle iron at the ferroxidase center.

102 al cavity through a process facilitated by a ferroxidase center.

103 te at 48 Zn(2+)per 24mer, i.e., 2 Zn(2+) per ferroxidase center.

104 ccurs at a diiron binding center, termed the ferroxidase center.

105 serves as a port of entry for Fe(2+) to the ferroxidase center.

106 ecies are transferred into the core from the ferroxidase center.

107 from Fe(2+) oxidation in the cavity, to the ferroxidase center.

108 be used to monitor the loss of iron from the ferroxidase center.

109 t catalytic dinuclear iron center called the ferroxidase center.

110 was also sensitive to the iron status of the ferroxidase center.

111 on of Fe(2+) across the protein shell to the ferroxidase center.

112 only avenues for rapid Fe(2+) access to the ferroxidase center.

113 pared in which Trp34 was introduced near the ferroxidase center.

114 a dinuclear metal-binding site known as the "ferroxidase center." The chemistry of Fe(II) binding and

115 a new model for Fe(II) translocation to the ferroxidase center: self-assembly creates channels that

116 The MD simulations also show that Pa BfrB ferroxidase centers are highly dynamic and permanently p

117 tion, aa residues that comprise the putative ferroxidase centers generally are not conserved, suggest

118 ron mineralization is initiated at dinuclear ferroxidase centers inside the protein where Fe(2+) and

119 of the expected peroxo complex forms at the ferroxidase centers of HoSF when two Fe(II)/H-subunits a

120 Additionally only one-half of the 24 ferroxidase centers of MtF are functional, further contr

121 rolysis chemistry despite their similar diFe ferroxidase centers.

122 or the diffusion of iron and dioxygen to the ferroxidase centers.

123 To determine whether the ferroxidase ceruloplasmin (Cp) and its homolog hephaesti

124 AMD were identified in mice deficient in the ferroxidase ceruloplasmin (Cp) and its homologue hephaes

125 e 2 metals is the liver-derived, multicopper ferroxidase ceruloplasmin (Cp) that is important for iro

126 ron overload disease due to mutations in the ferroxidase ceruloplasmin (Cp).

127 se the Wilson protein delivers copper to the ferroxidase ceruloplasmin in the liver, it is likely tha

128 Apart from the ferroxidase ceruloplasmin, all are involved in myelin ho

129 neurons (PN) where it delivers copper to the ferroxidase ceruloplasmin.

130 t sequence identity to the serum multicopper ferroxidase ceruloplasmin.

131 ally expressed band revealed identity to the ferroxidase ceruloplasmin.

132 The mammalian ferroxidases ceruloplasmin and hephaestin are homologs o

133 Outside the cell, a multi-copper ferroxidase, ceruloplasmin (Cp), oxidizes ferrous to fer

134 Fe(2)O-P](Z) represents an oxidized diferric ferroxidase complex, probably a mu-oxo-bridged species a

135 (III)(2)O-P](Z) a micro-oxo-bridged diferric ferroxidase complex.

136 ge Z and [Fe(2)-P](Z) represents a diferrous ferroxidase complex.

137 s DNA, whereas neither the L-subunit nor the ferroxidase-deficient 222-mutant of the H-subunit has de

138 ptake as shown by the ineffectiveness of two ferroxidase-deficient Cp preparations, copper-deficient

139 ferrin was critical for iron release because ferroxidase-deficient Cp was inactive and because holotr

140 om macrophages under hypoxic conditions by a ferroxidase-dependent mechanism, possibly involving gene

141 functionally homologous to the S. cerevisiae ferroxidase, does not have enough similarity to interact

142 ent the structure of the Fet3p extracellular ferroxidase domain and compare it with that of human cer

143 The absence of a conserved ferroxidase domain and the potentiation of oxidative str

144 Direct identification of ferritin ferroxidase (F(ox)) sites, complicated by multiple types

145 rt system, such as a deletion in the surface ferroxidase FET3, also result in increased metal sensiti

146 pletion of extracellular Fe(II) by the yeast ferroxidase Fet3p or iron chelators can maintain cell su

147 e yeast plasma membrane (PM) consists of the ferroxidase, Fet3p, and the ferric iron permease, Ftr1p.

148 changed with the TM domain from the vacuolar ferroxidase, Fet5p, with no loss of assembly and traffic

149 haestin (Heph), a membrane-bound multicopper ferroxidase (FOX) expressed in duodenal enterocytes, is

150 -bond network appear to distinguish a fungal ferroxidase from a fungal laccase since the specificity

151 eruloplasminemic mice because of the loss of ferroxidase function.

152 r, these data allow a molecular movie of the ferroxidase gating mechanism to be developed and provide

153 ll poorly understood, and insect multicopper ferroxidases have not been identified.

154 ntioxidant function is mainly related to its ferroxidase I (FeOxI) activity, which influences iron-de

155 ion of copper proteins like plastocyanin and ferroxidase in copper-replete medium and for apoplastocy

156 cells because ectopic expression of SOD2 and ferroxidase in Mirk-depleted cells lowered ROS levels.

157 Instead, loss of ferroxidases in other retinal cells causes retinal iron

158 n the RPE cells does not result from loss of ferroxidases in the photoreceptors, and Cp and Heph play

159 mouse, hephaestin (basolateral multi-copper ferroxidase) in the sex-linked anaemic mouse (sla) and f

160 CRR1 in copper distribution to a multicopper ferroxidase involved in iron assimilation.

161 cating that the ability of Fet3p to act as a ferroxidase involves other amino acids.

162 possible pathway for the internalization of ferroxidase iron into the interior cavity of Pa FtnA.

163 conformation that enables coordination to a ferroxidase iron.

164 Ceruloplasmin, a Cu-containing ferroxidase, is found at higher levels in UTI urine than

165 Fet3, the apparent ferroxidase, is proposed to facilitate iron uptake by ca

166 While EncFtn acts as a ferroxidase, it cannot mineralize iron.

167 The ferroxidase ligands (except His130) are poised to bind i

168 isiae, we identify the two of five candidate ferroxidases likely involved in high-affinity Fe-uptake

169 Multicopper ferroxidases (MCFs) play an important role in cellular i

170 ucture of the type 1 Cu site of Fet3p to the ferroxidase mechanism, we have examined the absorption,

171 Ferroxidase-mediated loading of iron into apotransferrin

172 They correspond to the ferroxidase, mineral surface, and the Fe(II) + H2O2 deto

173 Hephaestin is a membrane-bound multicopper ferroxidase necessary for iron egress from intestinal en

174 that the hephaestin protein is a multicopper ferroxidase necessary for iron egress from intestinal en

175 A ferroxidase-negative Fet3p did not suppress the copper s

176 raction, no interaction between heterologous ferroxidase permease pairs was observed.

177 We constructed the analogous ferroxidase, permease chimera and demonstrate that it su

178 rt by the combined activity of Smf3p and the ferroxidase, permease pair of proteins, Fet5p and Fth1p.

179 n measurements in solution, suggest that the ferroxidase pore is the dominant entry route for the upt

180 s the Pa BfrB shell via B-pores and that the ferroxidase pores allow the capture and oxidation of Fe(

181 Ceruloplasmin (Cp), a ferroxidase present in the cerebrospinal fluid (CSF), co

182 Hephaestin (Heph) is a ferroxidase protein that converts ferrous to ferric iron

183 The H-subunit catalyzed ferroxidase reaction 1 occurs at all levels of iron load

184 None were active in the essential ferroxidase reaction catalyzed by Fet3p.

185 y two sequential iron oxidation reactions: A ferroxidase reaction catalyzed by mYfh1p induces the fir

186 lation and acts as substrate for Fet3 in the ferroxidase reaction catalyzed by this ceruloplasmin hom

187 Kinetic analysis of the in vitro ferroxidase reaction catalyzed by this soluble Fet3p yie

188 irst detectable reaction intermediate of the ferroxidase reaction is a diferric-peroxo intermediate,

189 lso lost rapidly when the solution pH of the ferroxidase reaction is controlled by a pH stat apparatu

190 ted rapid loss of H(2)O(2) produced from the ferroxidase reaction of ferritin is unlikely due to reac

191 Oxidative degradation of mYfh1p during the ferroxidase reaction suggests that most H(2)O(2) reacts

192 to Fe(III) at the type 1 copper; this is the ferroxidase reaction that is fundamental to the physiolo

193 ectroscopy were used to monitor the ferritin ferroxidase reaction using recombinant (apo) frog M ferr

194 A ferroxidase reaction with a stoichiometry of 2 Fe(II)/O(

195 rom O(2) is rapidly consumed in a subsequent ferroxidase reaction with Fe(II) to produce H(2)O.

196 xidation of ferrous ion by molecular oxygen (ferroxidase reaction) at a binuclear site (ferroxidase s

197 ron to provide a large driving force for the ferroxidase reaction, while still supporting the deliver

198 reduction of O(2) to H(2)O and is termed the ferroxidase reaction.

199 ry implies production of H(2)O(2) during the ferroxidase reaction.

200 The ferroxidase site (FS) bound iron is then oxidized accord

201 sidue in close proximity to the iron-binding ferroxidase site (W52 in E. coli Dps).

202 mino acid side chains in the vicinity of the ferroxidase site and along the D helix to the three-fold

203 t variant A1 retains a completely functional ferroxidase site and has iron oxidation and mineralizati

204 show a clear distinction between the diiron ferroxidase site and mineral surface catalyzed oxidation

205 First, rather than a ferroxidase site at the subunit interface, as is observe

206 idized form of the protein has a symmetrical ferroxidase site containing two five-coordinate iron ato

207 ncrease in the average Fe-Fe distance in the ferroxidase site from approximately 3.5 to approximately

208 dation/hydrolysis reaction attributed to the ferroxidase site has been determined for the first time

209 binding of ferrous iron and dioxygen to the ferroxidase site in preparation for catalysis and a part

210 s is observed in all other DPS proteins, the ferroxidase site in SsDPSL is buried within the four-hel

211 the first time, the diferric species at the ferroxidase site is identified in ferritins from higher

212 ereby the peroxo intermediate decays and the ferroxidase site is postulated to vacate its complement

213 the first mechanism, turnover of iron at the ferroxidase site is rapid, resulting in steady-state pro

214 ite variant A1 (E64A/E67A) which retains the ferroxidase site ligand Glu61.

215 A diiron ferroxidase site located on the H-chain subunit of verte

216 l produced from Fenton chemistry whereas the ferroxidase site mutant 222 (H62K + H65G) and human L-ch

217 d impairment may be due to disruption of the ferroxidase site of the protein since Glu61 is a shared

218 > 2Fe(O)OH(core) + 4H(+)] that occurs at the ferroxidase site of the protein, thereby preventing the

219 formed during Fe(II) oxidation by O2 at the ferroxidase site of the protein.

220 urnover of Fe(III) at this site and that the ferroxidase site plays a role in catalysis at all levels

221 ) in excess of that required to saturate the ferroxidase site promotes rapid turnover of Fe(III) at t

222 d satisfactorily by a mechanism in which the ferroxidase site rapidly produces an incipient core from

223 ound within hydrogen bonding distance of the ferroxidase site that bridges the two iron atoms on the

224 dation/hydrolysis increasingly shifts from a ferroxidase site to a mineral surface based mechanism, d

225 The transfer of iron from the ferroxidase site to the mineral core has been now establ

226 These proteins have a catalytic site, "the ferroxidase site", located on the H-type subunit that fa

227 (ferroxidase reaction) at a binuclear site (ferroxidase site) found in each of the 24 subunits.

228 ng sites within an iron-uptake channel and a ferroxidase site, common features related to the canonic

229 Fe(2+) ions at a dinuclear site, called the ferroxidase site, located within each of the 24 subunits

230 ase corresponding to Fe(II) oxidation at the ferroxidase site, which is saturated after adding 48 fer

231 n product of Dps with one iron bound at each ferroxidase site.

232 eralization through the activity of a diiron ferroxidase site.

233 n mineralization and demonstrates a flexible ferroxidase site.

234 nce that H(2)O(2) is produced at this diiron ferroxidase site.

235 peculiar features of divalent cations at the ferroxidase site.

236 Specifically, a dinuclear (ferroxidase) site, a b-type heme site, and the binding o

237 ns bind at each of the 12 putative dinuclear ferroxidase sites (P(Z)) in the protein according to the

238 Fe(2+) binding, transport, and oxidation at ferroxidase sites and mineralization of a hydrous ferric

239 ariants lacking functional nucleation and/or ferroxidase sites deposit their iron largely through the

240 that matches precisely their location at the ferroxidase sites determined earlier by X-ray crystallog

241 wever, because of the relatively few H-chain ferroxidase sites in HoSF and the reaction of H(2)O(2) w

242 corresponding to the proposed path from the ferroxidase sites to the mineral nucleation sites along

243 gesting a similar mechanism for the ferritin ferroxidase step in all fast ferritins.

244 asing transcription of the antioxidant genes ferroxidase, superoxide dismutase (SOD)2, and SOD3.

245 Ceruloplasmin is a serum ferroxidase that contains greater than 95% of the copper

246 Ceruloplasmin (Cp) is a copper-containing ferroxidase that functions as an antioxidant in part by

247 Ceruloplasmin is an iron-export ferroxidase that is abundant in plasma and also expresse

248 Fet3p is a ferroxidase that, like ceruloplasmin and hephaestin, cou

249 protein is known to function as an essential ferroxidase, the role of ceruloplasmin in copper transpo

250 The requirement for a ferroxidase to maintain iron transport activity represen

251 Fpn requires the action of an exocytoplasmic ferroxidase, which can be either endogenous Hp or extrac

252 er may enhance biosynthesis of a circulating ferroxidase, which potentiates iron release from stores.

253 , LPR1 (LOW PHOSPHATE ROOT1) and LPR2 encode ferroxidases, which when mutated, reduce Fe(3+) accumula

254 This result indicates that the S. pombe ferroxidase, while functionally homologous to the S. cer