ライフサイエンスコーパス: ferroxidase

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

2 lux in the presence of an active multicopper ferroxidase.

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

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

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

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

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

8 iated with an upregulation of iron-exporting ferroxidases.

9 tions are distinct from those of other known ferroxidases.

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

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

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

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

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

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

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

17 as demonstrated to exhibit phenoloxidase and ferroxidase activities.

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

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

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

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

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

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

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

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

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

27 is was evident in decreased copper-dependent ferroxidase activity despite increased abundance of the

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

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

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

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

32 The ferroxidase activity of the ferritin H chain is critical

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

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

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

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

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

38 Cp ferroxidase activity was required for iron uptake as sho

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

40 nificant in Fe metabolism enabling efficient ferroxidase activity while avoiding ROS generation.

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

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

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

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

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

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

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

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

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

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

51 ther multicopper oxidases that are devoid of ferroxidase activity.

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

53 essing conserved amino acids responsible for ferroxidase activity.

54 aMCO3, that likely contribute to the overall ferroxidase activity.

55 ting DNA binding under conditions of ongoing ferroxidase activity.

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

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

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

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

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

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

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

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

64 PHATE RESPONSE1 (LPR1), a cell wall-targeted ferroxidase, and PHOSPHATE DEFICIENCY RESPONSE2 (PDR2),

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

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

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

68 that the acquisition of bacterial LPR1-type ferroxidase by embryophyte progenitors facilitated the e

69 table T = 4 shell topology and its catalytic ferroxidase cargo and show interactions underlying cargo

70 se of the differences in organization of the ferroxidase catalytic site and neighboring secondary met

71 Multicopper ferroxidases catalyze the oxidation of ferrous iron to f

72 h O(2) and H(2) O(2) can oxidize iron at the ferroxidase center (FC) of Escherichia coli bacterioferr

73 This involves a mixed-valent ferroxidase center (MVFC) that is readily detected under

74 ich both serves to attract metal ions to the ferroxidase center and acts as a flow-restricting valve

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

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

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

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

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

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

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

82 We show that catalysis occurs in the ferroxidase center and suggest a dual role for the secon

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

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

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

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

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

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

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

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

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

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

93 lar mechanism by which substrate flux to the ferroxidase center is controlled, potentially to ensure

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

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

96 First, its catalytic diiron ferroxidase center is unlike those of all other characte

97 in, Fe(2+) oxidation at the catalytic diiron ferroxidase center of FtMt proceeds via a distinct mecha

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

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

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

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

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

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

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

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

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

107 24 subunits, to a di-iron binding site, the ferroxidase center, buried in the middle of each active

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

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

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

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

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

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

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

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

116 t catalytic dinuclear iron center called the ferroxidase center.

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

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

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

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

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

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

123 n the two-helix subunits and proximal to the ferroxidase center.

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

125 stricting valve to limit the activity of the ferroxidase center.

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

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

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

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

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

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

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

133 ze the oxidation of Fe(2+) at binuclear iron ferroxidase centers (FOC) and store the Fe(3+) in their

134 cC form rotationally symmetric decamers with ferroxidase centers (FOCs) that oxidize Fe(+2) to Fe(+3)

135 the different oxidative steps of the various ferroxidase centers already known in ferritins were succ

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

137 the product of O(2) reduction, implying that ferroxidase centers function in pairs via long-range ele

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

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

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

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

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

143 rolysis chemistry despite their similar diFe ferroxidase centers.

144 motifs in bacterioferritins, the di-nuclear ferroxidase centre and the haem B group, play key roles

145 mineral core, which is dependent on the heme-ferroxidase centre electron transfer pathway.

146 The ferroxidase centre is known to be required for the rapid

147 rapid electron transfer between the heme and ferroxidase centre of bacterioferritin from Escherichia

148 release kinetics, which demonstrate that the ferroxidase centre plays an important role in the reduct

149 ectron transfer pathway from the haem to the ferroxidase centre suggesting a new role(s) haem might p

150 in-type ferritins harbour a diiron site, the ferroxidase centre, at the centre of a 4 alpha-helical b

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

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

153 We selected the ferroxidase Ceruloplasmin (CP) as an exemplary gene to d

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

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

156 the iron exporter, ferroportin (Fpn) and the ferroxidase ceruloplasmin (Cp).

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

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

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

160 t sequence identity to the serum multicopper ferroxidase ceruloplasmin.

161 ally expressed band revealed identity to the ferroxidase ceruloplasmin.

162 The mammalian ferroxidases ceruloplasmin and hephaestin are homologs o

163 activity despite increased abundance of the ferroxidases ceruloplasmin and hephaestin.

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

165 cted processes such as those associated with ferroxidase complex, high-affinity iron-permease complex

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

183 mbryophytes (land plants) acquired LPR1-type ferroxidase from soil bacteria via horizontal gene trans

184 eruloplasminemic mice because of the loss of ferroxidase function.

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

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

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

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

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

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

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

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

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

194 ltered iron homeostasis identifies CP, a key ferroxidase involved in systemic iron distribution by ca

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

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

197 conformation that enables coordination to a ferroxidase iron.

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

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

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

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

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

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

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

205 Ferroxidase-mediated loading of iron into apotransferrin

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

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

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

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

210 i sensing in root meristems, encodes a novel ferroxidase of high substrate specificity and affinity (

211 ach in R. irregularis to find genes encoding ferroxidases of the multicopper oxidase (MCO) gene famil

212 O) gene family in an attempt to identify the ferroxidase partner of RiFTR1.

213 apable of transporting Fe in yeast without a ferroxidase partner, resembling the Fe transport mechani

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

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

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

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

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

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

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

221 ins, peroxidasins, antioxidant enzymes and a ferroxidase protein.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

257 > 2Fe(O)OH(core) + 4H(+)] that occurs at the ferroxidase site of the protein, thereby preventing the

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

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

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

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

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

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

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

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

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

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

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

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

270 n mineralization and demonstrates a flexible ferroxidase site.

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

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

273 eralization through the activity of a diiron ferroxidase site.

274 peculiar features of divalent cations at the ferroxidase site.

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

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

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

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

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

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

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

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

283 rated that RiMCO1 and RiMCO3 can function as ferroxidases, suggesting their involvement in the reduct

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

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

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

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

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

289 sporter, ferroportin (Fpn) and a multicopper ferroxidase, that is, hephaestin (Heph), ceruloplasmin (

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

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

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

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

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

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