ライフサイエンスコーパス: iron-sulfur protein

1 on of the C-terminal extrinsic domain of the iron sulfur protein.

2 reaction complex between quinol and oxidized iron sulfur protein.

3 o the pKa values of cytochrome bH and Rieske iron sulfur protein.

4 reduction potential of the active site in an iron-sulfur protein.

5 anous helix close to the hinge region of the iron-sulfur protein.

6 ty to induce mobile or fixed conformation of iron-sulfur protein.

7 arrB is predicted to encode a 25.7-kDa iron-sulfur protein.

8 complex, where it interacts with the Rieske iron-sulfur protein.

9 upon the rate of ubiquinol oxidation by the iron-sulfur protein.

10 lipid phase and the extrinsic domain of the iron-sulfur protein.

11 ritical for maintaining the stability of the iron-sulfur protein.

12 me c1, and an amino-terminal fragment of the iron-sulfur protein.

13 t Ala-185 of cytochrome b interacts with the iron-sulfur protein.

14 ich is a pyridoxamine 5'-phosphate dependent iron-sulfur protein.

15 e quinone portal and the hinge region of the iron-sulfur protein.

16 gene cluster including an alternative Rieske iron-sulfur protein.

17 hanges were typical of those in other 4Fe-4S iron sulfur proteins.

18 reminiscent of those found in molybdenum and iron sulfur proteins.

19 ers, and participates in the biosynthesis of iron-sulfur proteins.

20 3, 4) clusters that form the active sites of iron-sulfur proteins.

21 nds in modulating the reduction potential of iron-sulfur proteins.

22 a sequence motif similar to a motif found in iron-sulfur proteins.

23 ation states of the metal centers in several iron-sulfur proteins.

24 a thioredoxin-like fold that is novel among iron-sulfur proteins.

25 acellular concentration of iron by attacking iron-sulfur proteins.

26 n Arabidopsis, required for full activity of iron-sulfur proteins.

27 gene involved in the maturation of cytosolic iron-sulfur proteins.

28 e domain capable of binding two tetranuclear iron-sulfur proteins.

29 ine dinucleotide] dehydrogenase [ubiquinone] iron-sulfur protein 1) or other mitochondrial subunits p

30 evels of the NADH dehydrogenase (ubiquinone) iron-sulfur protein 3, NADH dehydrogenase (ubiquinone) 1

31 hich encodes NADH dehydrogenase (ubiquinone) iron-sulfur protein 4, results in compromised activity o

32 has a UV-visible spectrum characteristic of iron-sulfur proteins (410 nm (11.9 mM(-1) cm(-1)) and 45

33 e also decreased the levels of the corrinoid iron-sulfur protein (60%) and methyltransferase (70%).

34 ing anaerobic growth and inactivation of the iron-sulfur proteins, aconitase and fumarase, by accumul

35 These phenotypes include decreases in iron-sulfur protein activities coordinated with increase

36 for the involvement of yggX in protection of iron-sulfur proteins against oxidative damage.

37 are any sequence similarity with the classic iron-sulfur proteins, although four cysteines (which are

38 ion of sirC and sirD, encoding a periplasmic iron sulfur protein and an integral membrane hydroquinon

39 none, or class I inhibitors, and the reduced iron sulfur protein and formation of a reaction complex

40 ne 5'-phosphosulfate reductase (MtAPR) is an iron-sulfur protein and a validated target to develop ne

41 sine-5'-phosphosulfate (APS) reductase is an iron-sulfur protein and a validated target to develop ne

42 gent electron transfer from ubiquinol to the iron-sulfur protein and cytochrome b(L) within the cytoc

43 quinol must simultaneously interact with the iron-sulfur protein and cytochrome b.

44 s bifurcated electron transfer to the Rieske iron-sulfur protein and cytochrome b.

45 idase site, but that interaction between the iron-sulfur protein and cytochrome c1 is partially impai

46 e the high potential centers of complex III (iron-sulfur protein and cytochromes c + c1), NADH or suc

47 llin with H-bonds between H161 of the Rieske iron-sulfur protein and E272 of the cyt b protein.

48 e oxidation reflected the pK on the oxidized iron-sulfur protein and requirement for the deprotonated

49 the loss of F(X), F(B), and F(A), the Rieske iron-sulfur protein and the non-heme iron in photosystem

50 f iron dealt with here include biogenesis of iron-sulfur proteins and chaperones that deliver iron co

51 (iii) Iron-sulfur proteins and charge clusters.

52 properties of the Fe(III)-thiolate bonds of iron-sulfur proteins and corroborating the important rol

53 fs1p in assembly/maturation of mitochondrial iron-sulfur proteins and that one or more of the target

54 relevance, as many pathogens sense NO using iron-sulfur proteins and will be exposed to NO in an aer

55 ng terminal cytochrome oxidases, inactivates iron/sulfur proteins, and promotes entry into latency.

56 ype yeast, even though normal amounts of the iron-sulfur protein are present as judged by Western blo

57 of the protein to the redox potential in an iron-sulfur protein are studied via energy minimization,

58 sequences of the S. pombe and S. cerevisiae iron-sulfur proteins are 50% identical, with the highest

59 Iron-sulfur proteins are among the primary targets of ni

60 Iron-sulfur proteins are among the sensitive targets of

61 Iron-sulfur proteins are found in all life forms.

62 s a high degree of similarity to a number of iron-sulfur proteins as well as to the beta subunit of g

63 electron transfer chain, with the cytosolic iron-sulfur protein assembly (CIA) machinery required fo

64 O1), an essential component of the cytosolic iron-sulfur protein assembly (CIA) machinery, is crucial

65 morsin complex, a component of the cytosolic iron-sulfur protein assembly (CIA) machinery.

66 The T. hominis cytosolic iron-sulfur protein assembly (CIA) pathway includes the

67 The final step of iron-sulfur protein assembly involves transfer of an iro

68 ur cluster machinery (ISC) and a cytoplasmic iron-sulfur protein assembly machinery (CIA).

69 In the cytosolic iron-sulfur protein assembly machinery, two human key pr

70 , is an essential component of the cytosolic iron-sulfur protein assembly pathway in yeast.

71 c protein that plays a role in the cytosolic iron-sulfur protein assembly pathway.

72 9 can simultaneously bind probable cytosolic iron-sulfur protein assembly protein CIAO1 and Fe-S prot

73 rocesses such as transcription, translation, iron-sulfur protein assembly, nucleotide metabolism, LPS

74 paramagnetic resonance (EPR) spectrum of the iron sulfur protein, associated with its interactions wi

75 reduction of cytochrome c(1) and the Rieske iron-sulfur protein at center P.

76 evealed by the structures, a movement of the iron sulfur protein between two separate reaction domain

77 ochondrial components required for cytosolic iron sulfur protein biogenesis.

78 r a human homologue of IscA, named IscA1, in iron-sulfur protein biogenesis.

79 iation with genes proposed to be involved in iron-sulfur protein biosynthesis.

80 amma display folds related to high potential iron-sulfur proteins but differ substantially from each

81 n of the complex, including oxidation of the iron sulfur protein by cytochrome c(1) and the reactions

82 uced in SMP via cytochrome c, and the Rieske iron-sulfur protein by ascorbate and faster by ascorbate

83 r-185 in the Saccharomyces cerevisiae Rieske iron-sulfur protein by site-directed mutagenesis of the

84 cum catalyzes the methylation of a corrinoid/iron-sulfur protein (C/Fe-SP) by the N5 methyl group of

85 These results establish that mature-sized iron-sulfur protein can be formed by single-step process

86 nt of movement of the head domain of reduced iron-sulfur protein, caused by disruption of electron tr

87 tween methyltransferase (MeTr) and corrinoid iron-sulfur protein (CFeSP) are required for the transfe

88 The corrinoid iron-sulfur protein (CFeSP) from Clostridium thermoaceti

89 etrahydrofolate (CH(3)-H(4)folate) corrinoid-iron-sulfur protein (CFeSP) methyltransferase (MeTr) cat

90 ve studied the axial ligation of a corrinoid iron-sulfur protein (CFeSP) that plays a key role in ene

91 t(III) species on one protein (the corrinoid iron-sulfur protein (CFeSP)) to a nickel iron-sulfur clu

92 te) to the cob(I)amide center of a corrinoid/iron-sulfur protein (CFeSP), forming H4folate and methyl

93 4folate) to the cobalt center of a corrinoid/iron-sulfur protein (CFeSP), forming methylcob(III)amide

94 sis from CoA, CO, and a methylated corrinoid iron-sulfur protein (CFeSP).

95 from the CH(3)-Co(3+) site in the corrinoid iron-sulfur protein (CFeSP).

96 [FeFe]-hydrogenases are iron-sulfur proteins characterized by a complex active s

97 CoA, and a methyl group bound to a corrinoid-iron sulfur protein (CoFeSP).

98 nd a methyl group donated from the corrinoid-iron-sulfur protein (CoFeSP).

99 transferred onto the enzyme from a corrinoid-iron-sulfur protein (CoFeSP).

100 The corrinoid-iron/sulfur protein (CoFeSP) operates within the reducti

101 e first comprehensive characterization of an iron-sulfur protein complex that regulates Spo0A approxi

102 haves similarly to stigmatellin, inducing an iron-sulfur protein conformational arrest.

103 Western blotting analyses reveal a reduced iron-sulfur protein content in Y268S bc(1) suggestive of

104 cluster affects molecular properties of the iron-sulfur protein, crystal structures of reduced C73S

105 IR and visible redox difference spectra of iron-sulfur protein/cytochrome c(1), heme b(H), and heme

106 (class II), and a distal domain close to the iron sulfur protein docking interface, where stigmatelli

107 ferredoxin by (i) sparing iron for abundant iron-sulfur proteins essential for acetotrophic growth a

108 Iron-sulfur proteins exhibited loss of iron cofactors, y

109 sulate the semiquinone from oxidation by the iron-sulfur protein, explaining the efficiency of bifurc

110 The motion of the Rieske iron-sulfur protein extrinsic domain, essential for elec

111 Miner2 is a member of a new CDGSH iron-sulfur protein family that also includes two mitoch

112 Electron transfer between the Rieske iron-sulfur protein (Fe(2)S(2)) and cytochrome c(1) was

113 a NO-responsive Wbl protein (actinobacterial iron-sulfur proteins first identified in the 1970s).

114 D, a member of the WhiB-like (Wbl) family of iron-sulfur proteins found exclusively within the actino

115 e occupancies of different positions for the iron sulfur protein from the crystallographic electron d

116 raises the midpoint potential of the Rieske iron-sulfur protein from 285 to 385 mV, and shifts the g

117 act efficiently in vitro with high potential iron-sulfur protein from A. vinosum (Em +350 mV).

118 x and facilitate dissociation of the reduced iron-sulfur protein from Pdr, and (iii) transfer of an e

119 protein by site-directed mutagenesis of the iron-sulfur protein gene to examine how these hydrogen b

120 d by site-directed mutagenesis of the cloned iron-sulfur protein gene, so that the recognition sites

121 to transform yeast cells (JPJ1) lacking the iron-sulfur protein gene.

122 us experiments using deletion mutants of the iron-sulfur protein had indicated that amino acid residu

123 A range of iron-sulfur proteins has been found to accommodate these

124 , -Ser) in Chromatium vinosum high-potential iron sulfur protein have been examined with the aim of u

125 reactions that contribute to movement of the iron sulfur protein have been measured and shown to be l

126 major effect on the interaction between the iron-sulfur protein headgroup and the quinol oxidation s

127 ene, pioC, encodes a putative high potential iron sulfur protein (HiPIP) with a twin-arginine translo

128 -sulfur cluster motif in both high potential iron-sulfur protein (HiPIP) and ferredoxin (Fd) active s

129 n contrast, the C. purpuratum high-potential iron-sulfur protein (HiPIP) differs from those isolated

130 demonstrate in vivo that the high potential iron-sulfur protein (HiPIP) from Allochromatium vinosum

131 The crystal structure of the high-potential iron-sulfur protein (HiPIP) isolated from Chromatium pur

132 trate, generating an oxidized high potential iron-sulfur protein (HiPIP)-like intermediate.

133 oxin (Fd), and to new data on high-potential iron-sulfur protein (HiPIP).

134 trophic growth, including two high-potential iron-sulfur proteins (HiPIPs) (PioC and Rpal_4085) and a

135 eins, the rubredoxins and the high-potential iron-sulfur proteins (HiPIPs), no structural explanation

136 ependent formate dehydrogenase-H), and three iron-sulfur proteins: HycB, HycF, and HycG.

137 Three iron-sulfur proteins--HydE, HydF, and HydG--play a key r

138 and bc1 complexes indicate that intermediate iron-sulfur protein (i-ISP) has full activity when compa

139 he parameters determining the binding of the iron sulfur protein in different configurations.

140 terference of the complex III subunit Rieske iron sulfur protein in the cytochrome b-null cells and t

141 t Ser-175 of cytochrome b is shielded by the iron-sulfur protein in the bc1 complex.

142 Import of S. pombe iron-sulfur protein in which the putative MIP or MPP rec

143 g high concentrations of metal chelators and iron-sulfur protein in which the recognition site for th

144 Iron-sulfur protein in which the recognition site for th

145 Possible roles for these iron-sulfur proteins in electron transport and light har

146 x exists as a dimer with intertwining Rieske iron-sulfur proteins in solution, four Rhodobacter sphae

147 , three pathways exist for the maturation of iron-sulfur proteins in the cytosol, plastids, and mitoc

148 hese strains accumulated intermediate length iron-sulfur proteins in vivo.

149 NEET proteins belong to a unique family of iron-sulfur proteins in which the 2Fe-2S cluster is coor

150 mitochondrial cytochrome bc1 complex we used iron-sulfur proteins in which the presequences had been

151 minished activity of cytosolic aconitase, an iron-sulfur protein, in liver extracts.

152 diminished activity of various mitochondrial iron-sulfur proteins including aconitase.

153 e deletion strain complemented with S. pombe iron-sulfur protein indicate that the S. pombe protein i

154 The crystal structure of the bovine Rieske iron-sulfur protein indicates a sulfur atom (S-1) of the

155 at the same conserved docking surface on the iron sulfur protein interacts with cytochrome c(1) and w

156 d by site-directed mutagenesis and import of iron-sulfur protein into mitochondria from yeast mutants

157 are critical for the proper assembly of the iron-sulfur protein into the bc1 complex.

158 is necessary for import and assembly of the iron-sulfur protein into the cytochrome bc1 complex, we

159 roline together with EDTA inhibits import of iron-sulfur protein into the matrix space of mitochondri

160 correlation between the import of the Rieske iron-sulfur protein into the mitochondrial matrix and pr

161 These results indicate that import of the iron-sulfur protein into the mitochondrial matrix is ind

162 Many iron-sulfur proteins involved in cluster trafficking for

163 The protein is homologous to B(12)-dependent iron-sulfur proteins involved in halorespiration.

164 f this complex are the flavoprotein (Fp) and iron-sulfur protein (Ip) of the dehydrogenase, and two i

165 The membrane-bound Rieske iron-sulfur protein is an essential component of the cyt

166 At pH 8.8, where the redox potential of the iron-sulfur protein is approximately 200 mV and in a bc(

167 otein in a single step, and the mature-sized iron-sulfur protein is correctly targeted to the outer s

168 yeast strain JPJ1, in which the gene for the iron-sulfur protein is deleted, was transformed with the

169 strain in which the endogenous gene for the iron-sulfur protein is deleted.

170 The [2Fe-2S] cluster of the Rieske iron-sulfur protein is held between two loops of the pro

171 When iron-sulfur protein is imported into mitochondria in vit

172 ate that one step processing of the S. pombe iron-sulfur protein is independent of those sites and of

173 ng that movement of the tether region of the iron-sulfur protein is necessary for maximum rates of en

174 egrees for Chromatium vinosum high-potential iron-sulfur protein is predicted to be in good agreement

175 ce of this recognition sequence the S. pombe iron-sulfur protein is processed only once during import

176 However, when the iron-sulfur protein is removed from the S175C-substitute

177 onfirming that oxidation of ubiquinol by the iron-sulfur protein is the rate-limiting partial reactio

178 The biogenesis of iron-sulfur proteins is a complex process that has becom

179 after import in vitro and of the endogenous iron-sulfur protein isolated from mitochondrial membrane

180 It was postulated that the iron-sulfur protein (ISP) accepts the first electron fro

181 in the interface between the head domain of iron-sulfur protein (ISP) and cytochrome b and the other

182 KCN to reduce the high potential components (iron-sulfur protein (ISP) and cytochrome c(1)) of comple

183 vitro between soluble domains of the Rieske iron-sulfur protein (ISP) and cytochrome f subunits of t

184 ion of the rate of Q(o)H(2) oxidation by the iron-sulfur protein (ISP) as well as the donation of ele

185 ectron transfer from ubiquinol to the Rieske iron-sulfur protein (ISP) at the Q(o)-site.

186 l movement of the soluble head of the Rieske iron-sulfur protein (ISP) between reaction domains in cy

187 Long-range movement of the Rieske iron-sulfur protein (ISP) between the cytochrome (cyt) b

188 rome bc(1) complex, the swivel motion of the iron-sulfur protein (ISP) between two redox sites consti

189 etween quinol bound at the Q(o) site and the iron-sulfur protein (ISP) docked at an interface on cyto

190 d the cyt bc1 complexes incorporate 'Rieske' iron-sulfur protein (ISP) domain movements to gate elect

191 iality of head domain movement of the Rieske iron-sulfur protein (ISP) during bc(1) catalysis, Rhodob

192 vided evidence that a movement of the Rieske iron-sulfur protein (ISP) extrinsic domain is essential

193 an electron from the [2Fe-2S] cluster of the iron-sulfur protein (ISP) extrinsic domain to the cytoch

194 ere, we report the observation of the Rieske iron-sulfur protein (ISP) in a mobile state, as revealed

195 (1) Q(o) site inhibitor that immobilizes the iron-sulfur protein (ISP) in the b conformation.

196 nted cyt b(6)f complex shows that the Rieske iron-sulfur protein (ISP) is in distinct orientations, d

197 he extramembrane (head) domain of the Rieske iron-sulfur protein (ISP) is involved in electron transf

198 that a large amplitude motion of the Rieske iron-sulfur protein (ISP) is required to mediate electro

199 he extramembrane domain (head) of the Rieske iron-sulfur protein (ISP) may play an important role in

200 at the soluble domain of the [2Fe-2S] Rieske iron-sulfur protein (ISP) must rotate by ca. 60 degrees

201 Sequence alignment of the Rieske iron-sulfur protein (ISP) of cytochrome bc(1) complex fr

202 he redox-linked protonation chemistry of the iron-sulfur protein (ISP) of the cytochrome bc(1) comple

203 In the Rieske iron-sulfur protein (ISP) of the ubiquinol:cytochrome c(

204 e inhibitor, inhibits electron transfer from iron-sulfur protein (ISP) to cytochrome c1 in the bc1 co

205 x suggests that the extra membrane domain of iron-sulfur protein (ISP) undergoes substantial movement

206 One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory

207 mobility of the extramembrane domain of the iron-sulfur protein (ISP): Binding of 5-undecyl-6-hydrox

208 s a large scale movement of a head domain of iron-sulfur protein (ISP-HD), which functionally connect

209 on with the RBD1 gene, which encodes a small iron-sulfur protein known as a rubredoxin.

210 y-deficient yeast strain due to formation of iron-sulfur protein lacking the iron-sulfur cluster.

211 in mutants of Synechococcus sp. PCC 7002 at iron sulfur protein-Leu-111 near the cluster.

212 Human mitoNEET is a homodimeric iron-sulfur protein located in the outer mitochondrial m

213 vity when compared with that of mature sized iron-sulfur protein (m-ISP).

214 The methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) from Clostr

215 The methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) from Clostr

216 The methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase (MeTr) from Clostr

217 Thus, expression of the iron-sulfur protein mitochondrial aconitase and function

218 ructures show that all interactions with the iron sulfur protein must occur at the distal position.

219 was also not greatly affected by the Rieske iron-sulfur protein mutations Y156W, S154A, or S154A/Y15

220 me F(420)-reducing hydrogenase (FrcA) and an iron sulfur protein (MvrD).

221 y has been overlooked as a tool for studying iron-sulfur protein nitrosylation despite the fact that

222 High potential iron-sulfur protein not only acts as direct electron don

223 p-phenylenediamine via cytochrome c1 and the iron-sulfur protein of complex III (ISP).

224 200 mV and in a bc(1) complex with a mutated iron-sulfur protein of equally low redox potential, the

225 h a small interfering RNA against the Rieske iron-sulfur protein of mitochondrial complex III did not

226 post-translational processing of the Rieske iron-sulfur protein of Saccharomyces cerevisiae and its

227 -terminal polypeptide fragment of the Rieske iron-sulfur protein of the cytochrome b6f complex from s

228 The iron-sulfur protein of the cytochrome bc1 complex is one

229 alanine residues in the tether region of the iron-sulfur protein of the yeast cytochrome bc(1) comple

230 The iron-sulfur proteins of the cytochrome bc1 complexes of

231 C. elegans mutations that disrupt particular iron-sulfur proteins of the electron transport chain.

232 d be the result of an altered binding of the iron-sulfur protein on the complex.

233 of decreasing the midpoint potential of the iron-sulfur protein on the rates of cytochrome b reducti

234 he excess purified head domain of the Rieske iron-sulfur protein partially restored the proton-pumpin

235 s complex and (ii) acetylation of the Rieske iron-sulfur protein (PetC) at the N terminus, a post-tra

236 Iron-sulfur proteins play an essential role in a variety

237 Iron-sulfur proteins play an essential role in many biol

238 Iron-sulfur proteins play indispensable roles in a broad

239 When Rieske iron-sulfur protein precursor is used as substrate for r

240 ation G167E could hinder the movement of the iron-sulfur protein, probably by distorting the structur

241 Two of these are located on the "Rieske" iron-sulfur protein protein (ISP) while the third is fou

242 separate, one-electron-transfer steps to the iron-sulfur protein putidaredoxin (Pdx).

243 these requirements with regard to the Rieske iron-sulfur protein QcrA of Bacillus subtilis.

244 omplex lacking the head domain of the Rieske iron-sulfur protein, removed by thermolysin digestion, i

245 The movement of the iron sulfur protein represents a novel mechanism of elec

246 We functionally characterized the iron-sulfur protein required for NADH dehydrogenase (IND

247 generation was inhibited by knockdown of the iron-sulfur protein, Rieske, in complex III.

248 or transfecting siRNA for the mitochondrial iron-sulfur protein, Rieske.

249 hen engineered into the budding yeast Rieske iron-sulfur protein Rip1, revealing remarkable conservat

250 ate assembly intermediate lacking the Rieske iron-sulfur protein Rip1.

251 in mouse lung fibroblasts lacking the Rieske iron-sulfur protein (RISP knockout [KO]cells), one of th

252 ablation of the genes coding for the Rieske iron-sulfur protein (RISP) and COX10, respectively.

253 (SMC)-specific RyR2 knockout (KO) or Rieske iron-sulfur protein (RISP) knockdown inhibits the altere

254 -mediated conditional deletion of the Rieske iron-sulfur protein (RISP) of Complex III was generated.

255 a heart- and muscle-specific isoform; Reiske iron-sulfur protein (RISP), a ubiquitously expressed ele

256 the iron-sulfur center FeS4 in the simplest iron-sulfur protein rubredoxin as a model system to demo

257 stigated the unfolding pathways of the small iron-sulfur protein rubredoxin from Pyrococcus furiosus

258 e, the reversible unfolding-refolding of the iron-sulfur protein rubredoxin was observed directly usi

259 of iron from the active site of the simplest iron-sulfur protein, rubredoxin, at the single molecule

260 In other reactions of SAM with iron-sulfur proteins, SAM is irreversibly consumed to ge

261 We explain this effect by b566, iron-sulfur protein short-circuiting under these conditi

262 A large scale domain movement involving the iron-sulfur protein subunit is required for electron tra

263 bditis elegans isp-1 gene encodes the Rieske iron-sulfur protein subunit of cytochrome c oxidoreducta

264 Import of the Rieske iron-sulfur protein subunit of the cytochrome c reductas

265 The "Rieske" iron-sulfur protein subunit shows significant conformati

266 e orientation of the g-tensors of the Rieske iron-sulfur protein subunit was determined in a single c

267 tional switch of the extrinsic domain of the iron-sulfur protein subunit.

268 eduction in the hydrophilic flavoprotein and iron-sulfur protein subunits.

269 ding of putidaredoxin (C and L helices), the iron-sulfur protein that acts as the effector and reduct

270 e iron metabolism, partly because IRP1 is an iron-sulfur protein that functions mainly as a cytosolic

271 ma and delta subunits constitute a corrinoid iron-sulfur protein that is involved in the transmethyla

272 HcpR2 is an iron-sulfur protein that reacts with NO and O2 .

273 Biotin synthase is an iron-sulfur protein that utilizes AdoMet to catalyze the

274 atalysis and place LipA within the family of iron-sulfur proteins that utilize AdoMet for radical-bas

275 ed with small interfering RNA against Rieske iron sulfur protein, the hypoxia-mediated Na,K-ATPase de

276 chrome b forms, with cytochrome c(1) and the iron--sulfur protein, the catalytic core of this multime

277 ough members of the Archaea produce numerous iron-sulfur proteins, the major cluster assembly protein

278 For two types of iron-sulfur proteins, the rubredoxins and the high-poten

279 ond to the iron-sulfur cluster of the Rieske iron-sulfur protein to a cysteine results in a respirato

280 talyzed by MPP is blocked, causing precursor iron-sulfur protein to accumulate.

281 Despite the homology of this iron-sulfur protein to aconitase, previously studied hom

282 Electron transfer from the Rieske iron-sulfur protein to cytochrome c(1) (cyt c(1)) in the

283 mplex, we mutagenized the presequence of the iron-sulfur protein to eliminate the original MPP site a

284 Most P450s interact with flavoenzymes or iron-sulfur proteins to receive electrons from NAD(P)H.

285 and core domains, (iii) stabilization of the iron-sulfur protein transmembrane helix, (iv) n-side cha

286 unoblotting revealed that the content of the iron-sulfur protein was decreased proportionately in the

287 Import of this mutant iron-sulfur protein was inhibited by the same concentrat

288 RamA, a 60-kDa monomeric iron-sulfur protein, was isolated from Methanosarcina ba

289 mall hairpin RNA directed against the Rieske iron-sulfur protein, we show that site III of the mitoch

290 cids located in the alpha1-beta4 loop of the iron-sulfur protein were mutated to uncharged residues a

291 itochondrial matrix while, at the same time, iron-sulfur proteins were deficient.

292 3K mutant enabled selective reduction of the iron-sulfur protein which in turn allowed the IR redox d

293 Mutant iron-sulfur protein which is processed to mature size in

294 sis from CO, CoA, and a methylated corrinoid iron-sulfur protein, which acts as a methyl donor.

295 cate that the catalytic domain of the Rieske iron-sulfur protein, which carries the [2Fe-2S] cluster,

296 s constitute a new subclass in the family of iron-sulfur proteins, which are distinguished not only b

297 equivalent of bovine adrenodoxin, is a small iron-sulfur protein with one [2Fe-2S] cluster.

298 a2epsilonx) subunits and a 100-kDa corrinoid/iron-sulfur protein with the 60- and 58-kDa subunits (ga

299 m bromide and Triton X-100: a 200-kDa nickel/iron-sulfur protein with the 89- and 19-kDa (alpha2epsil

300 2NT, ISP alpha 2NT and ISP beta 2NT (ISP for iron-sulfur protein) with gene designations ntdAaAbAcAd.