ライフサイエンスコーパス: capsulatus

1 uence (amino acids D43 to S49 in Rhodobacter capsulatus).

2 ive pentose phosphate pathway in Rhodobacter capsulatus.

3 hotosynthesis gene expression in Rhodobacter capsulatus.

4 not required for expression of acxABC in R. capsulatus.

5 ng signals to enhance genetic exchange in R. capsulatus.

6 phaeroides are more complex than those of R. capsulatus.

7 t affect reducing equivalents in Rhodobacter capsulatus.

8 cofactor in DMSO reductase from Rhodobacter capsulatus.

9 during anaerobic photosynthetic growth of R. capsulatus.

10 nsulfur photosynthetic bacterium Rhodobacter capsulatus.

11 o-component regulatory system in Rhodobacter capsulatus.

12 ense, Rhodospirillum rubrum, and Rhodobacter capsulatus.

13 ive pentose phosphate pathway in Rhodobacter capsulatus.

14 in species of Rhizobiaceae or in Rhodobacter capsulatus.

15 reviously known cyt c biogenesis genes of R. capsulatus.

16 is in some gram-negative bacteria such as R. capsulatus.

17 d previously in a bc(1) complex mutant of R. capsulatus.

18 containing bacterium and a predecessor to R. capsulatus.

19 e to support the photosynthetic growth of R. capsulatus.

20 factors and RNA polymerase from Rhodobacter capsulatus.

21 r in photosynthetic membranes of Rhodobacter capsulatus.

22 the biogenesis of the cyt cbb3 oxidase of R. capsulatus.

23 active CcoN-CcoO subcomplex was found in R. capsulatus.

24 mbly but also regulates Cu homeostasis in R. capsulatus.

25 Bacillus cereus ATCC 10987 and Methylococcus capsulatus.

26 heme-apocytochrome c ligation complex in R. capsulatus.

27 l and carotenoid biosynthesis in Rhodobacter capsulatus.

28 her plsC316 nor plsC3498 was essential in R. capsulatus.

29 structure of thioredoxin-2 from Rhodobacter capsulatus.

30 f this non-phosphorus membrane lipid from R. capsulatus.

31 ochrome c oxidase (cbb3 -Cox) of Rhodobacter capsulatus.

32 hine lipid biosynthesis genes of Rhodobacter capsulatus.

33 of the photosynthetic bacterium Rhodobacter capsulatus.

34 al species, such as the GTA from Rhodobacter capsulatus.

35 purple photosynthetic bacterium Rhodobacter capsulatus.

36 taproteobacterium, 4 Mbp), and Methylococcus capsulatus (a gammaproteobacterium, 3.3 Mbp).

37 rent strain of R.sphaeroides and Rhodobacter capsulatus, a close relative of R. sphaeroides.

38 In gram-negative bacteria, like Rhodobacter capsulatus, about 10 membrane-bound components (CcmABCDE

39 The importance of manganese in Rhodobacter capsulatus acetone carboxylase has been established thro

40 the positioning of succinyl-CoA, Rhodobacter capsulatus ALAS Asn-85 has a proposed role in regulating

41 X-ray crystal structures of Rhodobacter capsulatus ALAS reveal that a conserved active site seri

42 M. capsulatus, along with other methanotrophs, has been the

43 These results suggest that the R. capsulatus alpha subunit is not important for RcNtrC int

44 hane monooxygenase (pMMO) from Methylococcus capsulatus and ammonia monooxygenase (AMO) of Nitrosomon

45 o encode C-8 vinyl reductases in Rhodobacter capsulatus and Arabidopsis thaliana, respectively.

46 GTA production in the bacterium Rhodobacter capsulatus and characterization of novel phages that pos

47 ergent photosynthetic organisms, Rhodobacter capsulatus and Heliophilum fasciatum.

48 flagellatus were more similar to those in M. capsulatus and M. extorquens than to the ones in the mor

49 A comparative analysis of R. capsulatus and other alpha-proteobacterial promoters wit

50 homoserine lactone production by Rhodobacter capsulatus and Paracoccus denitrificans.

51 e with large and small subunit genes from R. capsulatus and R. sphaeroides, also supported the unrela

52 Using mutant strains of Rhodobacter capsulatus and Rhodobacter sphaeroides in which the pufX

53 ment RubisCO deletion strains of Rhodobacter capsulatus and Rhodobacter sphaeroides under both photoh

54 tein encoded by the pufX gene of Rhodobacter capsulatus and Rhodobacter sphaeroides, has been further

55 e localized proton entry into the RCs of Rb. capsulatus and Rps. viridis as well as locate a site of

56 tence of a second metal site in RCs from Rb. capsulatus and Rps. viridis.

57 repressed in a B12 auxotroph of Rhodobacter capsulatus and that B12 regulation of gene expression is

58 d wild-type cytochrome c(2) from Rhodobacter capsulatus and the lysine 93 to proline mutant of cytoch

59 type xanthine dehydrogenase from Rhodobacter capsulatus and variants at Arg-310 in the active site ha

60 eria Rhodobacter sphaeroides and Rhodobacter capsulatus, and is essential in controlling the metaboli

61 acteria Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodopseudomonas viridis has been invest

62 Thus, RCs from Rb. sphaeroides, Rb. capsulatus, and Rps. viridis each have a structurally an

63 hydrogenase-related protein from Rhodobacter capsulatus, and the regulatory subunit from bovine pyruv

64 In this study, using Rhodobacter capsulatus apocytochrome c(2) as a Ccm substrate, we dem

65 peptide designed to serve as a model for R. capsulatus apocytochrome c(2) have also been carried out

66 Thus, no additional factors from R. capsulatus are necessary for the recognition of high-GC

67 ive pentose phosphate pathway in Rhodobacter capsulatus are organized in at least two operons, each p

68 DsbA-null and DsbB-null single mutants of R. capsulatus are Ps(+) and produce c-type cytochromes, unl

69 ts of the facultative phototroph Rhodobacter capsulatus are unable to grow under photosynthetic condi

70 icated that the cbbI and cbbII operons of R. capsulatus are within separate CbbR regulons.

71 hat some OlsA enzymes, like the enzyme of R. capsulatus, are bifunctional and involved in both membra

72 R. sphaeroides cyt cy can act at least in R. capsulatus as an electron carrier between the cyt bc1 co

73 ubunits (Bchl and BchN) were expressed in R. capsulatus as S tag fusion proteins that facilitated aff

74 mutants of Escherichia coli and Rhodobacter capsulatus bacterioferritins are unable to associate int

75 h antibodies against cytochrome P460 from M. capsulatus Bath indicated that the expression level of c

76 tion of the genome sequence of Methylococcus capsulatus Bath is an important event in molecular micro

77 at a cytochrome P460 similar to that from M. capsulatus Bath may be present in the type II methanotro

78 and used to identify a DNA fragment from M. capsulatus Bath that contains cyp, the gene encoding cyt

79 was used to identify a DNA fragment from M. capsulatus Bath that contains occ, the gene encoding cyt

80 ethane monooxygenase (pMMO) in Methylococcus capsulatus Bath was assessed by analysis of transcripts

81 e complex (NADH dehydrogenase [NDH]) from M. capsulatus Bath, along with NADH and duroquinol, to enzy

82 from the obligate methylotroph Methylococcus capsulatus Bath.

83 isolated from the methanotroph Methylococcus capsulatus Bath.

84 he methane-oxidizing bacterium Methylococcus capsulatus Bath.

85 We have purified pMMO from Methylococcus capsulatus (Bath) and detected activity.

86 encoding MMOR was cloned from Methylococcus capsulatus (Bath) and expressed in Escherichia coli in h

87 indings extend previous work on pMMO from M. capsulatus (Bath) and provide new insight into the funct

88 thane mono-oxygenase (sMMO) of Methylococcus capsulatus (Bath) catalyses the O2-dependent and NAD(P)H

89 hane monooxygenase system from Methylococcus capsulatus (Bath) catalyzes the oxidation of methane to

90 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) catalyzes the selective oxidation of m

91 X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibromomethane or

92 bstrate, catalyzed by MMO from Methylococcus capsulatus (Bath) gave only cubylmethanol as the product

93 have been identified, and the Methylococcus capsulatus (Bath) genome has been sequenced.

94 MmoS from M. capsulatus (Bath) has been cloned, expressed, and purifi

95 losinus trichosporium OB3b and Methylococcus capsulatus (Bath) have a similar secondary structure top

96 soluble methane monooxygenase (sMMO) from M. capsulatus (Bath) have clarified discrepancies that exis

97 genase hydroxylase (MMOH) from Methylococcus capsulatus (Bath) in frozen 4:1 buffer/glycerol solution

98 rystal structures of MMOH from Methylococcus capsulatus (Bath) in the diiron(II), diiron(III), and mi

99 ethane monooxygenase system of Methylococcus capsulatus (Bath) includes three protein components: a 2

100 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a multicomponent enzyme system requ

101 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath) is a three-component enzyme system tha

102 25) from the pseudothermophile Methylococcus capsulatus (Bath) is a three-component enzyme system tha

103 MmoS from Methylococcus capsulatus (Bath) is the multidomain sensor protein of a

104 ld very similar to the one found here for M. capsulatus (Bath) MMOR-Fd.

105 A mononuclear copper center present in M. capsulatus (Bath) pMMO is absent in M. trichosporium OB3

106 as a metal center occupied by zinc in the M. capsulatus (Bath) pMMO structure is occupied by copper i

107 ed previously in the crystal structure of M. capsulatus (Bath) pMMO.

108 ys on membrane-bound pMMO from Methylococcus capsulatus (Bath) reveal that zinc inhibits pMMO at two

109 DNA sequencing of the Methylococcus capsulatus (Bath) sMMO genes confirmed previously identi

110 By mapping these residues on to the M. capsulatus (Bath) sMMO hydroxylase crystal structure, fu

111 Western blot analysis of Methylococcus capsulatus (Bath) soluble cell extracts showed that MMOD

112 thane monooxygenase effector protein from M. capsulatus (Bath) than that from M. trichosporium OB3b.

113 of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 A.

114 By cultivating Methylococcus capsulatus (Bath) under methane stress conditions and hi

115 oxygenase (sMMO) isolated from Methylococcus capsulatus (Bath) utilizes a carboxylate-bridged diiron

116 ns of methanotrophs, including Methylococcus capsulatus (Bath), express a membrane-bound or particula

117 Using MMOH from Methylococccus capsulatus (Bath), the effects of MMOB and MMOD on metal

118 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (ToMO) from Pse

119 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath), toluene monooxygenase (ToMO) from Pse

120 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath).

121 hane monooxygenase (sMMO) from Methylococcus capsulatus (Bath).

122 dies have focused on pMMO from Methylococcus capsulatus (Bath).

123 O-C was purified recently from Methylococcus capsulatus (Bath).

124 MOR-FAD) of the reductase from Methylococcus capsulatus (Bath).

125 be the role of the hinge region, Rhodobacter capsulatus bc(1) complex was used as a model, and variou

126 etergent dispersed chromatophore-embedded R. capsulatus bc(1) complex, we demonstrated that while sti

127 was identified 127 bp upstream of acxA in R. capsulatus, but this activator lacked key features of si

128 in photosynthetic membranes from Rhodobacter capsulatus by using inhibitor titrations and ubiquinone

129 sulfoxide reductase (DMSOR) from Rhodobacter capsulatus catalyzes the conversion of dimethyl sulfoxid

130 of the CBB pathway and regulation of the R. capsulatus cbb genes were studied by using a combination

131 of the heme-Cu-containing subunit CcoN of R. capsulatus cbb(3)-Cox proceeds independently of that of

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

133 In contrast, the R. capsulatus ccdA was homologous to the cyt c biogenesis g

134 lecular genetic studies, we inferred that R. capsulatus CcmF, CcmH, and CcmI interact with each other

135 henotypes upon overproduction of the CcmF-R. capsulatus CcmH (CcmF-CcmH(Rc)) couple in a growth mediu

136 In R. capsulatus, CcmI-null mutants are unable to produce c-ty

137 sin, or an endogenous activity present in R. capsulatus, cleaves the hinge region of the Fe-S subunit

138 The nifR3-ntrB-ntrC operon in R. capsulatus codes for the nitrogen-sensing two component

139 460 and cytochromes c' in N. europaea and M. capsulatus, confirm the importance of a heme-crosslink t

140 ligation core complex, which in Rhodobacter capsulatus contains at least the CcmF, CcmH, and CcmI co

141 cultative phototrophic bacterium Rhodobacter capsulatus contains only one form of cytochrome (cyt) c

142 respiratory electron transfer, unlike its R. capsulatus counterpart, Cyt cyRc.

143 All R. capsulatus cycJ mutants studied so far excrete copious a

144 position L286 of the ef loop of Rhodobacter capsulatus cyt b could alleviate movement impairment res

145 ied Zn(2+)-induced inhibition of Rhodobacter capsulatus cyt bc(1) using enzyme kinetics, isothermal t

146 The latter residue is M183 in Rhodobacter capsulatus cyt c1, and previous mutagenesis studies reve

147 laced with Lys and five modified Rhodobacter capsulatus Cyt c2 molecules in which positively charged

148 Redox transitions in the Rhodobacter capsulatus cytochrome bc(1) complex were investigated by

149 cytochrome c(1) component of the Rhodobacter capsulatus cytochrome bc(1) complex, phenylalanine 138 a

150 and spectroscopic properties of Rhodobacter capsulatus cytochrome c' (RCCP) have been compared to da

151 n a conserved acidic patch (region 2) on Rb. capsulatus cytochrome c(1) suggests that these negativel

152 ly 34 and the adjacent Pro 35 of Rhodobacter capsulatus cytochrome c(2) (or Gly 29 and Pro 30 in vert

153 positions in the hinge region of Rhodobacter capsulatus cytochrome c(2) and have determined the struc

154 The mutation of Gly 34 to Ser in Rb. capsulatus cytochrome c(2) has been characterized in ter

155 In the case of Rhodobacter capsulatus cytochrome c(2), the sixth heme ligand Met96

156 ion constants for the binding of Rhodobacter capsulatus cytochrome c2 and its K93P mutant to the cyto

157 These results are consistent with R. capsulatus cytochrome c2 stabilizing the complex through

158 of imidazole to eight mutants of Rhodobacter capsulatus cytochrome c2 that differ in overall protein

159 ram-negative bacteria, including Rhodobacter capsulatus, cytochrome c maturation (Ccm) is carried out

160 photosynthetic bacterium Rhodobacter (Rba.) capsulatus, cytochrome c(1) contains two additional cyst

161 created in the background of the Rhodobacter capsulatus D(LL) mutant, in which the D helix of the M s

162 d anaerobic photoautotrophic growth of the R.capsulatus deletion strain with 5% CO(2), but not with 1

163 Genetic analysis of ccoGHIS in Rhodobacter capsulatus demonstrated that ccoG, ccoH, ccoI and ccoS a

164 es dimethyl sulfoxide reductase, Rhodobacter capsulatus dimethyl sulfoxide reductase, and Shewanella

165 d to act as an apocytochrome c chaperone, R. capsulatus does not have the ability to produce holocyto

166 We utilized R. capsulatus:E. coli hybrid RNA polymerases assembled in v

167 A kinetic isotope study of the wild-type R. capsulatus enzyme indicates that, as previously determin

168 In specific mutant strains of R. capsulatus, expression of both the Calvin-Benson-Bassham

169 lash photolysis and RCs from the Rhodobacter capsulatus F(L181)Y/Y(M208)F/L(M212)H mutant (designated

170 in the hinge region (positions 43-49) of R. capsulatus Fe-S subunit was not essential per se for the

171 the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR re

172 s confirm earlier results indicating that R. capsulatus ferrocytochrome c(2) exhibits minor rotationa

173 ile genetic manipulation, we purified the R. capsulatus form I enzyme and determined its basic kineti

174 The R. capsulatus form I enzyme was found to be subject to a ti

175 cently proposed phylogenetic placement of R. capsulatus form I RubisCO.

176 component regulatory system from Rhodobacter capsulatus functions as a global regulator of metabolic

177 An R. capsulatus gene responsible for long-chain acyl-homoseri

178 , resulted in decreased production of the R. capsulatus gene transfer agent, and gene transfer agent

179 Using a R. capsulatus genetic system, the cyt c1 mutants M183K and

180 utotrophicus and sequence analysis of the R. capsulatus genome and were found to be clustered in simi

181 The Rhodobacter capsulatus genome contains three genes (olsA [plsC138],

182 Depletion of manganese from the R. capsulatus growth medium resulted in inhibition of aceto

183 ndings therefore demonstrate that, during R. capsulatus growth on minimal medium, the requirement for

184 f either olsA or plsC316 was required for R. capsulatus growth under the conditions tested.

185 Among these species, Rhodobacter capsulatus has a periplasmic Cyt c2Rc and a membrane-bou

186 the purple non-sulfur bacterium Rhodobacter capsulatus have been carried out.

187 ontaining Me(2)SO reductase from Rhodobacter capsulatus have been examined spectroscopically and kine

188 the xanthine dehydrogenase from Rhodobacter capsulatus have been examined to ascertain whether Glu(2

189 The R. capsulatus HelX and Ccl2 proteins are predicted to funct

190 A Rhodobacter capsulatus hemC mutant has been isolated and used to sho

191 Phenotypic differences between the R.capsulatus host strain complemented with the wild-type r

192 rC enhancer-binding protein activates the R. capsulatus housekeeping RNA polymerase but not the Esche

193 Phenotypic analysis of the M. capsulatus hpnR deletion mutant demonstrated a potential

194 in a Rubisco deletion strain of Rhodobacter capsulatus identified a residue in the amino terminus of

195 orts efficiently photosynthetic growth of R. capsulatus in the absence of cyt c2 because it can media

196 y were in the proteobacterium, Methylococcus capsulatus, in which sterol biosynthesis is known, and i

197 cter sphaeroides, the form I RubisCO from R. capsulatus is a member of the green-like group and close

198 CrtJ from Rhodobacter capsulatus is a regulator of genes involved in the biosy

199 the cytochrome bc1 complex) from Rhodobacter capsulatus is composed of the Fe-S protein, cytochrome b

200 is study, we show that SenC from Rhodobacter capsulatus is involved in the assembly of a fully functi

201 mplementing them revealed that ccoNOQP in R. capsulatus is not flanked by the oxygen response regulat

202 ht harvesting gene expression in Rhodobacter capsulatus is repressed under aerobic growth conditions

203 t the expression of hem genes in Rhodobacter capsulatus is transcriptionally repressed in response to

204 The purple bacterium Rhodobacter capsulatus is unique among Rhodobacteriacae as it contai

205 om the photosynthetic bacterium, Rhodobacter capsulatus, is shown in vitro to activate the housekeepi

206 er, R. sphaeroides cyt cy, unlike that of R. capsulatus, is unable to function as an efficient electr

207 tive phototrophic (Ps) bacterium Rhodobacter capsulatus, it is constituted by the cyt b, cyt c1, and

208 operon essential for cyt c biogenesis, in R. capsulatus, it is located immediately downstream from ar

209 nts affected in cyt c oxidase activity in R. capsulatus led to the isolation of at least five classes

210 rum, while a synthetic analog of Rhodobacter capsulatus lipid A (B 975) requires both rsCD14 and rLBP

211 iator ADP had no effect on the ability of R. capsulatus LPS to stimulate NO production but significan

212 ms that govern the diverse means by which R. capsulatus maintains redox poise during photoheterotroph

213 The bacterium Rhodobacter capsulatus mediates this process by repressing expressio

214 membranes and cross-reacted with Rhodobactor capsulatus membranes.

215 ex in chromatophore membranes of Rhodobacter capsulatus mutants lacking the Rieske iron-sulfur (Fe-S)

216 Herein, using Rhodobacter capsulatus mutants that have modifications in the hinge

217 been trapped in two D(LL)-based Rhodobacter capsulatus mutants that have Tyr at position M208 and la

218 f -10 promoter mutants did not facilitate R. capsulatus NtrC activation of the nifA1 promoter by the

219 It was previously shown that the Rhodobacter capsulatus NtrC enhancer-binding protein activates the R

220 s, an additional barrier to activation by R. capsulatus NtrC exists, probably a lack of the proper R.

221 Rhodobacter capsulatus NtrC is an enhancer-binding protein that acti

222 The Rhodobacter capsulatus NtrC protein is a bacterial enhancer-binding

223 trC exists, probably a lack of the proper R. capsulatus NtrC-E. coli RNA polymerase (protein-protein)

224 of high-GC promoters or for activation by R. capsulatus NtrC.

225 ing 2 (LH2, B800-850) mutants of Rhodobacter capsulatus obtained by combinatorial mutagenesis to the

226 peptides of Rs. rubrum, Rb. sphaeroides, Rb. capsulatus, or Rps. viridis.

227 n carrying the G488A mutation produced in R. capsulatus over 30-fold higher beta-galactosidase activi

228 n in an E. coli plsC(Ts) mutant of either R. capsulatus plsC316 or olsA gene products supported growt

229 Rhodobacter capsulatus produces various c-type cytochromes using the

230 ytoene desaturase gene (crtI) of Rhodobacter capsulatus, producing carotenoids with shorter conjugate

231 occal phage straight phiPVL, two Rhodobacter capsulatus prophages and two Mycobacterium tuberculosis

232 Ccl2 (a soluble, truncated form of Ccl2) R. capsulatus proteins, respectively.

233 A mutant form of the Rhodobacter capsulatus PrrA homologue, whose activity is independent

234 Expression of the Rhodobacter capsulatus puc operon, which codes for structural polype

235 ore segment containing 43 amino acids of Rb. capsulatus PufX exhibited 59 and 55% alpha-helix in trif

236 o inhibited by low concentrations of the Rb. capsulatus PufX protein (approximately 50% inhibition at

237 f the C-terminus) of Rb. sphaeroides and Rb. capsulatus PufX were chemically synthesized.

238 M polypeptide, M43(44) and M231(233) in Rb. capsulatus (Rb. sphaeroides).

239 ) is created in this manner in a Rhodobacter capsulatus RC containing the F(L181)Y-Y(M208)F-L(M212)H-

240 ormate dehydrogenase enzyme from Rhodobacter capsulatus (RcFDH) by means of hydrophobic interactions.

241 A large scale mutation of the Rhodobacter capsulatus reaction center M-subunit gene, sym2-1, has b

242 e primary charge separation processes in Rb. capsulatus reaction centers (RCs) bearing the mutations

243 ies are reported for a series of Rhodobacter capsulatus reaction centers (RCs) containing mutations a

244 y electron transfer reactions in Rhodobacter capsulatus reaction centers (RCs) having four mutations:

245 separation events in a series of Rhodobacter capsulatus reaction centers (RCs) that have been genetic

246 A cosmid carrying the R. capsulatus reg locus was capable of complementing an R.

247 DNase I footprint analyses, using R. capsulatus RegA*, a constitutively active mutant version

248 the purple non-sulfur bacterium Rhodobacter capsulatus, RegA and RegB comprise a two-component regul

249 Rhodobacter capsulatus regulates many metabolic processes in respons

250 , and Q in purple photosynthetic Rhodobacter capsulatus results in hydroquinone oxidation rates that

251 In Rhodobacter capsulatus, ribulose 1,5-bisphosphate carboxylase-oxygen

252 d in vitro to form an active, recombinant R. capsulatus RNA polymerase with properties mimicking thos

253 straints on how RcNtrC interacts with the R. capsulatus RNA polymerase.

254 Rhodobacter capsulatus SB 1003 belongs to the group of purple nonsul

255 s genetically tractable relative Rhodobacter capsulatus SB1003.

256 responded to the same metabolic signal in R. capsulatus SBI/II and mutant strain backgrounds.

257 of the photosynthetic bacterium Rhodobacter capsulatus served as a host.

258 otein that activates transcription of the R. capsulatus sigma 70 RNA polymerase, but does not activat

259 It is proposed that RcNtrC recruits R. capsulatus sigma 70-RNA polymerase to the promoter throu

260 The addition of R. capsulatus sigma(70) to the E. coli core RNA polymerase

261 roides, like the closely related Rhodobacter capsulatus species, contains both the previously charact

262 n in the obligate methanotroph Methylococcus capsulatus strain Bath.

263 A transposon mutant of Rhodobacter capsulatus, strain Mal7, that was incapable of photoauto

264 reported that mutant strains of Rhodobacter capsulatus that have alanine insertions (+nAla mutants)

265 Here, we show in Rhodobacter capsulatus that in the absence of DsbA cytochrome c leve

266 ene transfer agents of bacterium Rhodobacter capsulatus that transfer random 4.5-kbp (1.5 mum) DNA se

267 This finding demonstrates that in R. capsulatus the dithiol:disulfide oxidoreductases DsbA an

268 to be Ps(+) Nadi(+), establishing that in R. capsulatus the inactivation of dsbA suppresses the c-typ

269 ram-negative bacteria, including Rhodobacter capsulatus, the membrane protein CycH acts as a putative

270 lude to studies of cbb gene regulation in R. capsulatus, the nucleotide sequence of a 4,537-bp region

271 the LH1 alpha- and beta-polypeptides of Rb. capsulatus, the PufX protein of Rb. capsulatus was inhib

272 urple, photosynthetic bacterium, Rhodobacter capsulatus, the RegB/RegA two-component system is requir

273 In Rhodobacter capsulatus, the soluble cytochrome (cyt) c2 and membrane

274 For DMSOR from Rhodobacter capsulatus, thiolate dissociation has therefore been inv

275 In this study, the ability of Rhodobacter capsulatus to maintain a balanced intracellular oxidatio

276 n which mutants incapable of complementing R.capsulatus to photoautotrophic growth with 5% CO(2) were

277 tation assays between E.coli and Rhodobacter capsulatus to show that, despite their differences in si

278 ins either greatly reduced the ability of R. capsulatus to support growth or had little effect, respe

279 chrome c, leading in the case of Rhodobacter capsulatus to the loss of photosynthetic proficiency and

280 To facilitate studies of R. capsulatus transcription, we cloned and overexpressed al

281 In Rhodobacter capsulatus, two open reading frames (ORFs) carry the gen

282 Gram-negative bacteria like Rhodobacter capsulatus use intertwined pathways to carry out the pos

283 i-site of the cyt bc1 complex of Rhodobacter capsulatus using atomistic molecular dynamics simulation

284 brane topology of CcdA was established in R. capsulatus using ccdA:phoA and ccdA :lacZ gene fusions.

285 Rhodobacter capsulatus utilizes two terminal oxidases for aerobic re

286 e alpha- and beta-polypeptides of LH1 of Rb. capsulatus was also inhibited by low concentrations of t

287 ino acid sequencing, the PufX protein of Rb. capsulatus was identified, and from positive interaction

288 anthine dehydrogenase (XDH) from Rhodobacter capsulatus was immobilized on an edge-plane pyrolytic gr

289 s of Rb. capsulatus, the PufX protein of Rb. capsulatus was inhibitory to LH1 formation at low concen

290 nsulfur photosynthetic bacterium Rhodobacter capsulatus was purified to homogeneity and compared to t

291 oying the phototrophic bacterium Rhodobacter capsulatus was used to select a catalytically altered fo

292 DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will

293 s from Rhodobacter (Rb.) sphaeroides and Rb. capsulatus were carried out from pH 5 to 11.

294 These genes from Rhodobacter capsulatus were cloned separately into expression plasmi

295 eficient mutants, 771 and K2, of Rhodobacter capsulatus were isolated.

296 rom the photosynthetic bacterium Rhodobacter capsulatus, were obtained by specific interaction with a

297 rs (nifA1, nifA2, glnB, mopA and anfA) in R. capsulatus which are transcriptionally activated by NtrC

298 nown homolog is the bluB gene of Rhodobacter capsulatus, which is implicated in the biosynthesis of B

299 ired for glycerophospholipid synthesis in R. capsulatus, while olsA acts as an alternative AGPAT that

300 The ISP of Rhodobacter capsulatus within the intact cytochrome bc(1) complex wa