ライフサイエンスコーパス: Rhodobacter

1 genera such as Escherichia, Shewanella, and Rhodobacter, although TMAO reductases are present in man

2 se (CcO) and homologous prokaryotic forms of Rhodobacter and Paraccocus differ in the EPR spectrum of

3 ion of the formate dehydrogenase enzyme from Rhodobacter capsulatus (RcFDH) by means of hydrophobic i

4 The importance of manganese in Rhodobacter capsulatus acetone carboxylase has been esta

5 oordinating the positioning of succinyl-CoA, Rhodobacter capsulatus ALAS Asn-85 has a proposed role i

6 X-ray crystal structures of Rhodobacter capsulatus ALAS reveal that a conserved acti

7 n reported to encode C-8 vinyl reductases in Rhodobacter capsulatus and Arabidopsis thaliana, respect

8 tic basis of GTA production in the bacterium Rhodobacter capsulatus and characterization of novel pha

9 o highly divergent photosynthetic organisms, Rhodobacter capsulatus and Heliophilum fasciatum.

10 wn to complement RubisCO deletion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under

11 n is greatly repressed in a B12 auxotroph of Rhodobacter capsulatus and that B12 regulation of gene e

12 d and reduced wild-type cytochrome c(2) from Rhodobacter capsulatus and the lysine 93 to proline muta

13 ics of wild-type xanthine dehydrogenase from Rhodobacter capsulatus and variants at Arg-310 in the ac

14 In this study, using Rhodobacter capsulatus apocytochrome c(2) as a Ccm subst

15 A-null mutants of the facultative phototroph Rhodobacter capsulatus are unable to grow under photosyn

16 rg/Glu135Arg mutants of Escherichia coli and Rhodobacter capsulatus bacterioferritins are unable to a

17 The Rhodobacter capsulatus cbb(3)-type cytochrome c oxidase

18 by the heme ligation core complex, which in Rhodobacter capsulatus contains at least the CcmF, CcmH,

19 n located at position L286 of the ef loop of Rhodobacter capsulatus cyt b could alleviate movement im

20 rein we studied Zn(2+)-induced inhibition of Rhodobacter capsulatus cyt bc(1) using enzyme kinetics,

21 Redox transitions in the Rhodobacter capsulatus cytochrome bc(1) complex were inv

22 dues in the cytochrome c(1) component of the Rhodobacter capsulatus cytochrome bc(1) complex, phenyla

23 on chemistry and spectroscopic properties of Rhodobacter capsulatus cytochrome c' (RCCP) have been co

24 ations at 9 positions in the hinge region of Rhodobacter capsulatus cytochrome c(2) and have determin

25 In the case of Rhodobacter capsulatus cytochrome c(2), the sixth heme l

26 he dissociation constants for the binding of Rhodobacter capsulatus cytochrome c2 and its K93P mutant

27 RC) mutants created in the background of the Rhodobacter capsulatus D(LL) mutant, in which the D heli

28 R. sphaeroides dimethyl sulfoxide reductase, Rhodobacter capsulatus dimethyl sulfoxide reductase, and

29 nanosecond flash photolysis and RCs from the Rhodobacter capsulatus F(L181)Y/Y(M208)F/L(M212)H mutant

30 The Rhodobacter capsulatus genome contains three genes (olsA

31 molybdenum-containing Me(2)SO reductase from Rhodobacter capsulatus have been examined spectroscopica

32 Q variant of the xanthine dehydrogenase from Rhodobacter capsulatus have been examined to ascertain w

33 or selection in a Rubisco deletion strain of Rhodobacter capsulatus identified a residue in the amino

34 CrtJ from Rhodobacter capsulatus is a regulator of genes involved

35 In this study, we show that SenC from Rhodobacter capsulatus is involved in the assembly of a

36 onstrate that the expression of hem genes in Rhodobacter capsulatus is transcriptionally repressed in

37 The purple bacterium Rhodobacter capsulatus is unique among Rhodobacteriacae

38 The bacterium Rhodobacter capsulatus mediates this process by repressi

39 n center has been trapped in two D(LL)-based Rhodobacter capsulatus mutants that have Tyr at position

40 It was previously shown that the Rhodobacter capsulatus NtrC enhancer-binding protein act

41 Rhodobacter capsulatus NtrC is an enhancer-binding prote

42 Rhodobacter capsulatus produces various c-type cytochrom

43 e P(+)Q(B)(-) is created in this manner in a Rhodobacter capsulatus RC containing the F(L181)Y-Y(M208

44 f the primary electron transfer reactions in Rhodobacter capsulatus reaction centers (RCs) having fou

45 Rhodobacter capsulatus regulates many metabolic processe

46 , V, F, H, K, and Q in purple photosynthetic Rhodobacter capsulatus results in hydroquinone oxidation

47 Rhodobacter capsulatus SB 1003 belongs to the group of p

48 ressed in its genetically tractable relative Rhodobacter capsulatus SB1003.

49 etion mutant of the photosynthetic bacterium Rhodobacter capsulatus served as a host.

50 e previously reported that mutant strains of Rhodobacter capsulatus that have alanine insertions (+nA

51 Here, we show in Rhodobacter capsulatus that in the absence of DsbA cytoc

52 r-diameter gene transfer agents of bacterium Rhodobacter capsulatus that transfer random 4.5-kbp (1.5

53 to form cytochrome c, leading in the case of Rhodobacter capsulatus to the loss of photosynthetic pro

54 Gram-negative bacteria like Rhodobacter capsulatus use intertwined pathways to carry

55 eps at the Qi-site of the cyt bc1 complex of Rhodobacter capsulatus using atomistic molecular dynamic

56 Rhodobacter capsulatus utilizes two terminal oxidases fo

57 bacterial xanthine dehydrogenase (XDH) from Rhodobacter capsulatus was immobilized on an edge-plane

58 ubisco) employing the phototrophic bacterium Rhodobacter capsulatus was used to select a catalyticall

59 The ISP of Rhodobacter capsulatus within the intact cytochrome bc(1

60 In gram-negative bacteria, like Rhodobacter capsulatus, about 10 membrane-bound componen

61 purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and is essential in controlling

62 In many Gram-negative bacteria, including Rhodobacter capsulatus, cytochrome c maturation (Ccm) is

63 with the phytoene desaturase gene (crtI) of Rhodobacter capsulatus, producing carotenoids with short

64 In Gram-negative bacteria, including Rhodobacter capsulatus, the membrane protein CycH acts a

65 he closest known homolog is the bluB gene of Rhodobacter capsulatus, which is implicated in the biosy

66 b3 -type cytochrome c oxidase (cbb3 -Cox) of Rhodobacter capsulatus.

67 iochlorophyll and carotenoid biosynthesis in Rhodobacter capsulatus.

68 the crystal structure of thioredoxin-2 from Rhodobacter capsulatus.

69 to the ornithine lipid biosynthesis genes of Rhodobacter capsulatus.

70 ]hydrogenase of the photosynthetic bacterium Rhodobacter capsulatus.

71 ther bacterial species, such as the GTA from Rhodobacter capsulatus.

72 genes in the purple photosynthetic bacterium Rhodobacter capsulatus.

73 (CBB) reductive pentose phosphate pathway in Rhodobacter capsulatus.

74 illum brasilense, Rhodospirillum rubrum, and Rhodobacter capsulatus.

75 e iron oxidoreductase of the photoferrotroph Rhodobacter ferrooxidans SW2 was cloned, purified, and c

76 nalysis, demonstrated that these strains and Rhodobacter massiliensis represent a new genus, "Haemato

77 y alpha- and beta- proteobacteria, including Rhodobacter, Methylibium, Rhodopseudomonas, Methyloversa

78 nsfer of the cloned vbs genes, plus rpoI, to Rhodobacter, Paracoccus and Sinorhizobium conferred the

79 ls of Fe-removed/Zn-replaced RC protein from Rhodobacter ( R.) sphaeroides R26 were irradiated with v

80 In the LH2 proteins from Rhodobacter (Rb.) sphaeroides, the hydrogen bonds betwee

81 In the photosynthetic purple bacterium Rhodobacter (Rba.) sphaeroides, light is absorbed by mem

82 In Rhodobacter (Rba.) sphaeroides, the core complex contain

83 eme a (H102) is hydrogen bonded to serine in Rhodobacter (S44) and Paraccocus CcOs, in contrast to gl

84 a three-gene operon (the foxEYZ operon) from Rhodobacter sp. strain SW2 that confers enhanced light-d

85 a8c that overall was most similar to that of Rhodobacter species but was quite distinct from that of

86 nitrifying conditions as observed in another Rhodobacter species.

87 ynthase (HOS) and heme A synthase (HAS) from Rhodobacter sphaeroides (Cox10 and Cox15, respectively)

88 saccharide from the photosynthetic bacterium Rhodobacter sphaeroides (LPS-RS), a TLR4 inhibitor, prev

89 We found that the Argonaute of Rhodobacter sphaeroides (RsAgo) associates with 15-19 nt

90 xes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the q

91 Raman spectra of CcO from bovine (bCcO) and Rhodobacter sphaeroides (RsCcO).

92 res of a full-length LOV domain protein from Rhodobacter sphaeroides (RsLOV).

93 ); Mycobacterium tuberculosis (type II); and Rhodobacter sphaeroides (type III)] were tested for the

94 of similarity to the original pucBA genes of Rhodobacter sphaeroides 2.4.1 (designated puc1) was iden

95 2 complexes from the photosynthetic bacteria Rhodobacter sphaeroides 2.4.1 and Rhodopseudomonas acido

96 ulation of photosynthesis gene expression in Rhodobacter sphaeroides 2.4.1 have been well studied ove

97 Rhodobacter sphaeroides 2.4.1 is a facultative photohete

98 Rhodobacter sphaeroides 2.4.1 is a facultative photosynt

99 The hemF gene of Rhodobacter sphaeroides 2.4.1 is predicted to code for a

100 Part of the oxygen responsiveness of Rhodobacter sphaeroides 2.4.1 tetrapyrrole production in

101 hemA gene codes for one of two synthases in Rhodobacter sphaeroides 2.4.1 which catalyze the formati

102 The complex genome of Rhodobacter sphaeroides 2.4.1, composed of chromosomes I

103 ing sequence for PrrA, a global regulator in Rhodobacter sphaeroides 2.4.1, is poorly defined.

104 The rdxBHIS gene cluster of Rhodobacter sphaeroides 2.4.1, located downstream of the

105 vitro binding of PrrA, a global regulator in Rhodobacter sphaeroides 2.4.1, to the PrrA site 2, withi

106 he facultative phototrophic proteobacterium, Rhodobacter sphaeroides 2.4.1, was custom-designed and m

107 latory system is a major global regulator in Rhodobacter sphaeroides 2.4.1.

108 recent highlights taken from the studies of Rhodobacter sphaeroides 2.4.1.

109 photosynthetic reaction center isolated from Rhodobacter sphaeroides 2.4.1.

110 Analysis of the Rhodobacter sphaeroides 2.4.3 genome revealed four previ

111 The metabolically versatile purple bacterium Rhodobacter sphaeroides 2.4.3 is a denitrifier whose gen

112 The gene encoding this protein in Rhodobacter sphaeroides 2.4.3, designated cycP, was isol

113 was obtained from overexpressing variants of Rhodobacter sphaeroides 2.4.3.

114 ce of F6P) to the recombinant wild-type (WT) Rhodobacter sphaeroides adenosine 5'-diphosphate-(ADP)-g

115 previously observed in another TRAP-PBP (the Rhodobacter sphaeroides alpha-keto acid-binding protein)

116 ed-type RbcL subunits in the proteobacterium Rhodobacter sphaeroides also fold with GroEL/ES.

117 4, and 2.5 angstrom resolution) of TSPO from Rhodobacter sphaeroides and a mutant that mimics the hum

118 uced secondary quinone acceptor (Q(B)(-)) in Rhodobacter sphaeroides and Blastochloris viridis RCs.

119 lity assemblies are available: the bacterium Rhodobacter sphaeroides and chromosome 16 of the mouse g

120 o tracks obtained from the bacterial species Rhodobacter sphaeroides and Escherichia coli.

121 xidases and by the respiratory oxidases from Rhodobacter sphaeroides and Paracoccus denitrificans).

122 l transcription regulator in purple bacteria Rhodobacter sphaeroides and Rhodobacter capsulatus, and

123 Recently, Argonautes of the bacteria Rhodobacter sphaeroides and Thermus thermophilus were de

124 age the cytoplasmic chemoreceptor cluster in Rhodobacter sphaeroides and Vibrio cholerae.

125 the B12-binding domain family present in the Rhodobacter sphaeroides AppA protein binds heme and sens

126 of detergent-solubilized bc(1) complex from Rhodobacter sphaeroides are described.

127 n the photosynthetic reaction center (RC) of Rhodobacter sphaeroides are investigated by site-directe

128 window using the photosensory module of the Rhodobacter sphaeroides bacteriophytochrome BphG1 and th

129 The Rhodobacter sphaeroides bacteriophytochrome BphG1 is unc

130 Arg-94 in cytochrome b of the Rhodobacter sphaeroides bc(1) complex is fully conserved

131 obacterium tuberculosis genomes as well as a Rhodobacter sphaeroides benchmark dataset.

132 Rhodobacter sphaeroides biotin sulfoxide reductase (BSOR

133 he mapping of the photosynthetic membrane of Rhodobacter sphaeroides by atomic force microscopy (AFM)

134 Facultative phototrophs such as Rhodobacter sphaeroides can switch between heterotrophic

135 The reaction center (RC) from Rhodobacter sphaeroides captures light energy by electro

136 Anomalous difference Fourier analyses of Rhodobacter sphaeroides CcO crystals, with cadmium added

137 Rhodobacter sphaeroides cells contain curved membrane in

138 onstrate that FLAG-tagged PpsR isolated from Rhodobacter sphaeroides cells contains bound heme.

139 In Rhodobacter sphaeroides chromatophores, cytochromes (cyt

140 The chemosensory pathway of Rhodobacter sphaeroides comprises multiple homologues of

141 analysis of G78S, A200T and Delta F94-F98 in Rhodobacter sphaeroides confirmed and extended these obs

142 The cbb(3) cytochrome c oxidase of Rhodobacter sphaeroides consists of four nonidentical su

143 structure of a complex of BcsA and BcsB from Rhodobacter sphaeroides containing a translocating polys

144 measured in reaction centers from mutants of Rhodobacter sphaeroides containing a tyrosine residue ne

145 e of chromatophores isolated from strains of Rhodobacter sphaeroides containing light harvesting comp

146 on transfer were also studied in a series of Rhodobacter sphaeroides cyt bc(1) mutants involving resi

147 series of 21 mutants in the cyt b ef loop of Rhodobacter sphaeroides cyt bc1 were prepared to examine

148 For Rhodobacter sphaeroides CytcO (cytochrome aa3), it appea

149 ng methionine (M185) in cytochrome c1 of the Rhodobacter sphaeroides cytochrome bc1 complex with Lys

150 Binding of zinc to the outside surface of Rhodobacter sphaeroides cytochrome c oxidase inhibits th

151 ve mutant, E101A, in the K proton pathway of Rhodobacter sphaeroides cytochrome c oxidase.

152 ble residues around the BNC are evaluated in Rhodobacter sphaeroides cytochrome c oxidase.

153 d characterization of a series of mutants in Rhodobacter sphaeroides designed to reduce Q(B) via the

154 center (RC) of the photosynthetic bacterium Rhodobacter sphaeroides determines the rate and free ene

155 e (ICM) development process was performed in Rhodobacter sphaeroides during adaptation from high-inte

156 ivo and in vitro evidence that the genome of Rhodobacter sphaeroides encodes functional enzymes for C

157 The genome of Rhodobacter sphaeroides encodes the components of two di

158 Here, proton translocation by the Rhodobacter sphaeroides enzyme was studied using purifie

159 In the oxidized state both mutants of the Rhodobacter sphaeroides enzyme, D132A and K362M, show ov

160 The analogous site in Rhodobacter sphaeroides ETF-QO is asparagine 338.

161 n the vicinity of the iron-sulfur cluster of Rhodobacter sphaeroides ETF-QO.

162 the photosynthetic reaction center (RC) from Rhodobacter sphaeroides exhibits a cation-pi complex for

163 The LH1 and LH2 complexes of Rhodobacter sphaeroides form ring structures of 16 and 9

164 bilized at the Qi-site of the bc1 complex of Rhodobacter sphaeroides forms a hydrogen bond with a nit

165 de variants in a training set from a GC-rich Rhodobacter sphaeroides genome.

166 Rhodobacter sphaeroides grown in a Mn(II)-rich medium re

167 Rhodobacter sphaeroides has a complex chemosensory syste

168 Rhodobacter sphaeroides has a more complex chemotaxis sy

169 osynthetic membrane of the purple phototroph Rhodobacter sphaeroides has been characterised to a leve

170 cture of the light-harvesting I complex from Rhodobacter sphaeroides has been examined by site-direct

171 R from the anoxygenic phototrophic bacterium Rhodobacter sphaeroides has been known as an oxygen- and

172 ic reaction center from the purple bacterium Rhodobacter sphaeroides has been modified such that the

173 ve protochlorophyllide reductase (DPOR) from Rhodobacter sphaeroides has been purified from an Azotob

174 the transcriptional antirepressor AppA from Rhodobacter sphaeroides has been studied in the light an

175 n of the photosynthetic reaction center from Rhodobacter sphaeroides has been studied through the cha

176 Rhodobacter sphaeroides has both membrane-associated and

177 -electron tomography to the purple bacterium Rhodobacter sphaeroides has demonstrated a heretofore un

178 ochrome c oxidoreductase (EC 1.10.2.2)) from Rhodobacter sphaeroides have been characterized using el

179 Photosynthetic reaction centers from Rhodobacter sphaeroides have identical ubiquinone-10 mol

180 Previous studies of the oxidase from Rhodobacter sphaeroides have shown that all of the pumpe

181 Photosynthetic reaction centers from Rhodobacter sphaeroides have three ubiquinone-binding si

182 containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides have yielded new insight into it

183 ons of this extra fragment were generated in Rhodobacter sphaeroides in an effort to investigate its

184 n of the cytochrome c2-docked bc1 complex in Rhodobacter sphaeroides in terms of an ensemble of favor

185 cture for a translocator protein (TSPO) from Rhodobacter sphaeroides in which some of the electron de

186 The Rhodobacter sphaeroides intracytoplasmic membrane (ICM)

187 Rhodobacter sphaeroides is a metabolically diverse photo

188 BlrB in Rhodobacter sphaeroides is a single domain, flavin-based

189 The diheme cytochrome c (DHC) from Rhodobacter sphaeroides is a soluble protein with a mass

190 ranscriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV si

191 genes involved in photosystem development in Rhodobacter sphaeroides is dependent upon three major re

192 Z) of the facultative phototrophic bacterium Rhodobacter sphaeroides is induced upon a drop of oxygen

193 experiments have shown that ICM assembly in Rhodobacter sphaeroides is initiated at indentations of

194 Rhodobacter sphaeroides lipid A (RsDPLA) could not induc

195 1O2, we show that the phototrophic bacterium Rhodobacter sphaeroides mounts a transcriptional respons

196 n proton translocation of the bc(1) complex, Rhodobacter sphaeroides mutants expressing His-tagged cy

197 gment in bacterial cytochrome bc(1) complex, Rhodobacter sphaeroides mutants expressing His-tagged cy

198 ragment in bacterial cytochrome bc1 complex, Rhodobacter sphaeroides mutants expressing His-tagged cy

199 ion of quinol in the cytochrome bc1 complex, Rhodobacter sphaeroides mutants, H198N and H111N, lackin

200 structure of the axial mutant (Met182Thr) of Rhodobacter sphaeroides nitrite reductase in which the a

201 idic residue near the protein surface (D132, Rhodobacter sphaeroides numbering) and leads to another

202 An arginine (R481) (Rhodobacter sphaeroides numbering), positioned between t

203 ater and a pair of arginines, R481 and R482 (Rhodobacter sphaeroides numbering), that interact direct

204 annel is well-defined as D132(I) (subunit I; Rhodobacter sphaeroides numbering), the entrance of the

205 Three strains of Rhodobacter sphaeroides of diverse origin have been unde

206 eled ubiquinones in the Q(A) binding site in Rhodobacter sphaeroides photosynthetic reaction centers.

207 vesting 1 (LH1) integral membrane complex of Rhodobacter sphaeroides provides a convenient model syst

208 f SgTAM to the l-tyrosine ammonia lyase from Rhodobacter sphaeroides provides insight into the struct

209 RC) from the photosynthetic purple bacterium Rhodobacter sphaeroides R-26 were determined by fitting

210 ion center from the photosynthetic bacterium Rhodobacter sphaeroides R-26.

211 visible and near-infrared spectral region to Rhodobacter sphaeroides RCs to accurately track the timi

212 s during photosynthesis have been studied in Rhodobacter sphaeroides reaction centers from wild type

213 The Rhodobacter sphaeroides reaction centre is a relatively

214 ctron conduction across the highly tractable Rhodobacter sphaeroides reaction centre is characterized

215 nding processes in cytochrome c oxidase from Rhodobacter sphaeroides reduced to different degrees wer

216 210 in the photosynthetic reaction center of Rhodobacter sphaeroides results in the generation of a f

217 In a Rhodobacter sphaeroides ribulose 1,5-bisphosphate carbox

218 action centers (RCs) of the purple bacterium Rhodobacter sphaeroides runs selectively over one of the

219 39T mutant of translocator protein TSPO from Rhodobacter sphaeroides should be used to 1.65 instead o

220 Structures of the ISP from Rhodobacter sphaeroides show that serine 154 and tyrosin

221 the photosynthetic reaction center (RC) from Rhodobacter sphaeroides shows contacts between hydrophob

222 Rhodobacter sphaeroides sigma(E) is a member of the extr

223 The DNA sequences of chromosomes I and II of Rhodobacter sphaeroides strain 2.4.1 have been revised,

224 The denitrification phenotypes of Rhodobacter sphaeroides strains with and without norEF g

225 Rhodobacter sphaeroides synthesizes spheroidene as the m

226 cale TRN model for the alpha-Proteobacterium Rhodobacter sphaeroides that comprises 120 gene clusters

227 In RCs from Rhodobacter sphaeroides the protons involved in this pro

228 In the purple bacterium Rhodobacter sphaeroides the PSU forms spherical invagina

229 This work uses the model bacterium Rhodobacter sphaeroides to begin to elucidate how 3-hydr

230 by the photosynthetic alpha-proteobacterium Rhodobacter sphaeroides to procure the cobamide it needs

231 Cytochrome c(1) of Rhodobacter sphaeroides ubiquinol-cytochrome c oxidoredu

232 letion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under both photoheterotrophic an

233 The anoxygenic phototroph Rhodobacter sphaeroides uses 3-hydroxypropionate as a so

234 The aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides utilizes two proton-input channe

235 n photosynthetic reaction centers (RCs) from Rhodobacter sphaeroides was achieved by polarization sel

236 c(2) (cyt) and the reaction center (RC) from Rhodobacter sphaeroides was studied by mutation (to Ala)

237 from a magnesium chelatase (bchD) mutant of Rhodobacter sphaeroides were characterized.

238 ter from the purple photosynthetic bacterium Rhodobacter sphaeroides were covalently conjugated to ea

239 subtilis (expressed in Escherichia coli) and Rhodobacter sphaeroides were examined by analysis of cel

240 (P) in the photosynthetic reaction center of Rhodobacter sphaeroides were investigated by introducing

241 n kinetics of reaction centers isolated from Rhodobacter sphaeroides were shown to be inherently biph

242 heme protein from a denitrifying variant of Rhodobacter sphaeroides which may serve to store and tra

243 ated Rieske fragment from the bc1 complex of Rhodobacter sphaeroides with nitrogens (14N and 15N) fro

244 crystals of cytochrome c oxidase (CcO) from Rhodobacter sphaeroides yield a previously unreported st

245 copper-containing nitrite reductase (NiR) of Rhodobacter sphaeroides yielded endogenous NO and the Cu

246 ome c(2) to photosynthetic reaction centers (Rhodobacter sphaeroides) has been measured to high preci

247 these chromatophores can be spherical (as in Rhodobacter sphaeroides), lamellar (as in Rhodopseudomon

248 edox activity of individual purple bacteria (Rhodobacter sphaeroides).

249 In Rhodobacter sphaeroides, a photosynthetic alpha-proteoba

250 In the photosynthetic bacterium Rhodobacter sphaeroides, a transcriptional response to t

251 several sources (bovine heart mitochondria, Rhodobacter sphaeroides, and Paracoccus denitrificans).

252 he absorption spectrum of intact vesicles in Rhodobacter sphaeroides, as well as the well-established

253 Reaction centers from the Y(L167) mutant of Rhodobacter sphaeroides, containing a highly oxidizing b

254 Rhodobacter sphaeroides, for example, has multiple homol

255 e facultatively phototrophic proteobacterium Rhodobacter sphaeroides, formation of the photosynthetic

256 ction center in chromatophore membranes from Rhodobacter sphaeroides, have allowed us to demonstrate

257 In the purple phototrophic bacterium Rhodobacter sphaeroides, many protein complexes congrega

258 Calculations with structures of Rhodobacter sphaeroides, Paracoccus denitrificans, and b

259 agged membrane protein, Reaction Center from Rhodobacter sphaeroides, performed 2400 crystallization

260 In reaction centers of Rhodobacter sphaeroides, site-directed mutagenesis has i

261 enter (RC) from the photosynthetic bacterium Rhodobacter sphaeroides, that function in intermolecular

262 In the photosynthetic reaction center from Rhodobacter sphaeroides, the primary (Q(A)) and secondar

263 In Rhodobacter sphaeroides, the two cbb operons encoding du

264 otein, the light-harvesting LH2 complex from Rhodobacter sphaeroides, to patterned self-assembled mon

265 In the Q(A) site of RCs from Rhodobacter sphaeroides, ubiquinone-10 is reduced, by a

266 ying the carotenoidless mutant strain R26 of Rhodobacter sphaeroides, we demonstrate by experiment an

267 low-light-adapted chromatophore vesicle from Rhodobacter sphaeroides, we investigate the cooperation

268 oxidized forms of cytochrome c oxidase from Rhodobacter sphaeroides, we observe a displacement of he

269 me c maturation proteins, CcmF and CcmH from Rhodobacter sphaeroides, were analyzed.

270 l1 and Mcl2, two malyl-CoA lyase homologs in Rhodobacter sphaeroides, were investigated by gene inact

271 d by the genome of the alpha-proteobacterium Rhodobacter sphaeroides, which synthesizes a mitochondri

272 h surprising similarity to the fla2 locus of Rhodobacter sphaeroides.

273 at high and low pH in nitrite reductase from Rhodobacter sphaeroides.

274 sfer in single reaction center crystals from Rhodobacter sphaeroides.

275 n-Bassham CO(2) fixation pathway) operons of Rhodobacter sphaeroides.

276 ion of AppA, an oxygen and light sensor from Rhodobacter sphaeroides.

277 olog, RpoH(II), in the alpha-proteobacterium Rhodobacter sphaeroides.

278 ase PrrB in response to low oxygen levels in Rhodobacter sphaeroides.

279 beta-apoprotein from the core LH complex of Rhodobacter sphaeroides.

280 rates photosynthetic growth in the bacterium Rhodobacter sphaeroides.

281 photosynthesis in the alpha-proteobacterium Rhodobacter sphaeroides.

282 bb operons, responsible for CO2 fixation, in Rhodobacter sphaeroides.

283 gulator of photosynthesis gene expression in Rhodobacter sphaeroides.

284 anoic acid) (19Fu-FA), in phospholipids from Rhodobacter sphaeroides.

285 ic membranes from PufX+ and PufX- strains of Rhodobacter sphaeroides.

286 like that found in the alpha-proteobacterium Rhodobacter sphaeroides.

287 ssion of adhI, the gene encoding GSH-FDH, in Rhodobacter sphaeroides.

288 fixation pathway (cbbI and cbbII) operons of Rhodobacter sphaeroides.

289 esis gene expression in the purple bacterium Rhodobacter sphaeroides.

290 genes of the Calvin-Benson-Bassham cycle of Rhodobacter sphaeroides.

291 ntrast and fluorescence microscopy images of Rhodobacter sphaeroides.

292 ed from purified BcsA and BcsB proteins from Rhodobacter sphaeroides.

293 n a thriving culture of the purple bacteria, Rhodobacter sphaeroides.

294 been performed on cytochrome c oxidase from Rhodobacter sphaeroides.

295 oteins making up the split kinase, is met in Rhodobacter sphaeroides.

296 response of the bacterial reaction center of Rhodobacter sphaeroides.

297 film formation in the monotrichous bacterium Rhodobacter sphaeroides.

298 in detergent-solubilized bc(1) complex from Rhodobacter sphaeroides.

299 of mitochondria and many bacteria, including Rhodobacter sphaeroides.

300 Some of these LPS analogs (e.g. Rhodobacter spheroides LPS/lipid-A derivatives) are anta